Did you ever wonder what the finding so far are from the research done?
Below you will find each product we carry and the findings thus far. We will constantly update this page so be sure to check back often.


AICAR, aminoimidazole carboxamide ribonucleotide, acts as an agonist to AMP-activated protein kinase; AMP-activated protein kinase, also known as AMPK, is an enzyme with an important role in cellular homeostasis and energy regulation. AMPK acts through a variety of means to ultimately stimulate liver fatty oxidation, ketogenesis, beta-cell modulation of insulin secretion, and other functions within the body. AICAR has been shown to stimulate glucose uptake and reduce apoptosis by reducing reactive oxygen compounds within cells.

Buy Anastrozole from Progen Peptides (INN) (marketed under the trade name Arimidex by AstraZeneca) is a non-steroidal[3] aromatase-inhibiting drug approved for treatment of breast cancer after surgery, as well as for metastasis in both pre and post-menopausal women. The severity of breast cancer can be increased by estrogen, as sex hormones cause hyperplasia, and differentiation at estrogen receptor sites.[4] Anastrozole works by inhibiting the synthesis of estrogen. The patent on Arimidex by AstraZeneca expired June 2010.



The ATAC (Arimidex, Tamoxifen, Alone or in Combination) trial was an international randomised controlled trial of 9366 women with localized breast cancer who received either anastrozole, tamoxifen, or both for five years, followed by five years of follow-up.[5] After more than 5 years the group that received anastrozole had significantly better clinical results than the tamoxifen group.[5] The trial suggested that anastrozole is the preferred medical therapy for postmenopausal women with localized breast cancer, which is estrogen receptor (ER) positive.[5] Another study found that the risk of recurrence was reduced 40%, but was associated with an increased risk of bone fractures. The study concluded that ER positive patients benefited from switching from tamoxifen to anastrozole in patients who have completed 2 years’ adjuvant tamoxifen.[6] A more recent trial found that anastrozole significantly reduced the incidence of breast cancer in postmenopausal women relative to placebo, and while there were side effects related to estrogen deprivation observed, the researchers concluded that this was probably not related to the treatment. Lead author Jack Cuzick was quoted by the BBC as saying, “This class of drugs is more effective than previous drugs such as tamoxifen and crucially, it has fewer side effects,” adding that he thought there was now enough evidence to support offering the drug.[7]


Anastrozole binds reversibly to the aromatase enzyme through competitive inhibition, inhibits the conversion of androgens to estrogens in peripheral tissues (extra-gonadal).[8][9]


Bone weakness has been associated with anastrozole. Women who switched to anastrozole after two years on tamoxifen reported twice as many fractures as those who continued to take tamoxifen (2.1% compared to 1%).[6] Bisphosphonates are sometimes prescribed to prevent the osteoporosis induced by aromatase inhibitors. The level of circulating estradiol is likely causal here and not the anastrozole itself, and so the dose will determine likelihood of osteoporosis (estradiol inhibits osteoclasts, which resorb bone).


Anastrozole has been tested for reducing estrogens, including estradiol, in men.[10] Excess estradiol in men can cause benign prostatic hyperplasiagynecomastia, and symptoms of hypogonadism. It can also contribute to increased risk of stroke, heart attack, chronic inflammation, prostate enlargement and prostate cancer.[11] Some athletes and body builders use anastrozole as part of their steroid cycle to reduce and prevent symptoms of excess estrogen–gynecomastia, emotional lability and water retention.[10] Study data suggests dosages of 0.5 mg to 1 mg a day reduce serum estradiol approx. 50% in men, which differs in postmenopausal women.[12]


Anastrozole may be used off-label in children with precocious puberty, or children with pubertal gynecomastia.[13][2] Following the onset of puberty, the epiphyseal plate begins to close due to an increased amount ofestrogen production escaping local metabolism and spreading to the circulatory system.[13] It is shown to help slow this process, and increase adult height prediction in adolescent males treated with protein-based peptide hormones for the treatment of growth hormone deficiency.[14][14]


The synthesis begins with nucleophilic substitution of two benzylic bromides in α,α’-dibromomesitylene (prepared by radical bromination of mesitylene, not shown on the scheme) with cyanide by treatment with potassium cyanide under phase transfer conditions, affording the dinitrile. The resulting bis-nitrile in DMF was then deprotonated with sodium hydride in the presence of excess methyl iodide to give the bis-dimethylated product. Subsequently, a Wohl–Ziegler reaction was carried out using N-bromosuccinimide (NBS), and a catalytic amount of benzoyl peroxide (BPO) as the radical initiator. Finally, an SN2 displacement with sodium triazoleafforded anastrozole as a white solid.

Pentadecapeptide BPC 157, composed of 15 amino acids, is a partial sequence of body protection compound (BPC) that is discovered in and isolated from human gastric juice. Experimentally it has been demonstrated to accelerate the healing of many different wounds, including transected rat Achilles tendon. This study was designed to investigate the potential mechanism of BPC 157 to enhance healing of injured tendon. The outgrowth of tendon fibroblasts from tendon explants cultured with or without BPC 157 was examined. Results showed that BPC 157 significantly accelerated the outgrowth of tendon explants. Cell proliferation of cultured tendon fibroblasts derived from rat Achilles tendon was not directly affected by BPC 157 as evaluated by MTT assay. However, the survival of BPC 157-treated cells was significantly increased under the H2O2 stress. BPC 157 markedly increased the in vitro migration of tendon fibroblasts in a dose-dependent manner as revealed by transwell filter migration assay. BPC 157 also dose dependently accelerated the spreading of tendon fibroblasts on culture dishes. The F-actin formation as detected by FITC-phalloidin staining was induced in BPC 157-treated fibroblasts. The protein expression and activation of FAK and paxillin were determined by Western blot analysis, and the phosphorylation levels of both FAK and paxillin were dose dependently increased by BPC 157 while the total amounts of protein was unaltered. In conclusion, BPC 157 promotes the ex vivo outgrowth of tendon fibroblasts from tendon explants, cell survival under stress, and the in vitro migration of tendon fibroblasts, which is likely mediated by the activation of the FAK-paxillin pathway.

ACE-031 Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta)superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptorserine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptorsare all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, atransmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors areessential for signaling; and type II receptors are required for binding ligands and for expression of type Ireceptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type Ireceptors by type II receptors. Type II receptors are considered to be constitutively active kinases. This geneencodes activin A type IIB receptor, which displays a 3- to 4-fold higher affinity for the ligand than activin A typeII receptor.

Amyloid beta-protein/amyloid A4 or amyloid beta-peptide is derived from the amyloid beta-precursor protein. Beta amyloid is an extracellular filamentous protein deposit found in the brain. It is the major protein component of amyloid cores, neuritic plaques and is also found as a deposit in neurofibrillary tangles. In man, Alzheimer’s disease is the most common cause of senile dementia and is characterized by abnormal filamentous protein deposits in the brain. Beta amyloid deposits are also detected in Lewy body dementia, Down’s syndrome, amyloidosis (Dutch type) and in the Guam Parkinson-Dementia complex.

CJC 1295 with dac (synonym CJC1295/DAC, modified form (GRF 1-29) with drug affinity complex) belongs to class of tetrasubtituted peptide hormones and contains 30 amino acids; also it can be described as analog of GH releasing hormone. Its molecular formula is C165H269N47O46 and its molecular mass is 3647.28. CJC 1295 with DAC-complex was the first time developed and produced by Canadian scientists with initial purpose to find way to increase effective half-life period of growth hormone release hormone. The very first clinical studies regarding this research compound took place in the year of 2000. In 2006 a study concerning efficacy and effectiveness as well as safety profile of CJC 1295/DAC was done, it includes two double-blind, randomized, placebo-controlled trials. Due to having DAC-complex this research compound possesses greater binding affinity towards GHRH receptors, which in turn protects that hormone from degradation. CJC-1295 w/ dac-complex also stimulates production of hormone of growth and IGF-1 without increasing of prolactin, and that leads to effective fat loss. The same time it has ability to promote synthesis of proteins and therefore increasing growth of muscle tissues.

Mod GRF 1-29 In the healthy human body, large amounts of growth hormone are stored in the pituitary. The cells within the pituitary release growth hormone in response to signaling by GHRH (Growth Hormone Releasing Hormone), Ghrelin (of which GHRPs – Growth Hormone Releasing Peptides – are mimetics), and are inhibited from releasing these stores by Somatostatin. GHRH and Ghrelin act on different populations of somatotropes (GH releasing cells). GHRP/Ghrelin increases the number of somatotropes releasing GH but not the amount released by each cell; GHRH affects both the number of secreting cells and – more so – the amount they each secrete. [1] GHRH and Ghrelin are released in specific patterns that vary depending on event and environment: post-exercise, in response to slow wave sleep, in certain stages of life and physical development, and so on. Most people (even the diseased) continue to possess the ability to make GH in the pituitary. The problem is in the signalling of the pituitary to release it and make more. Even most people with diseases that affect growth hormone secretion retain the ability to continue to make GH in their pituitaries. The disease states and symptoms result, most typically, in altered (dysfunctional) GH release signaling and this also affects the ability of the pituitary to continue to make more GH. [2] Endogenous-type GHRH, which has a forty-four amino acid long chain (and a specific shape – thus making it a peptide as well as a hormone), has been marketed for the longest as Sermorelin in comparison to the other GHRH-type peptides. However, Sermorelin has been demonstrated to be degraded rapidly in the body and is cost-inefficient. But because most patients in need of GH therapy do retain the ability to produce and secrete their own GH, treatment with a GHRH-type analog remained hypothetically preferable to exogenous GH treatment. GH itself when administered exogenously results not only in “unnatural” release patterns, it results universally in down regulation of endogenous GH production – as do many hormones when applied exogenously.[3] Sermorelin’s limitations naturally resulted in a variety of formulations of GHRH analogs for therapeutic usage. CJC-1295, discussed in another article, is a GHRH analogue with attached MPA (aka DAC), binds to albumin in the bloodstream and circulates for a week or longer. Modified GRF 1-29, which is also called D-Ala2-GHRH-(1-29), [Nle27]-hGHRH(1-29)-NH2, GHRH (1-29)NH2, or ModGRF1-29, is the bioactive portion of GHRH(1-44) with fifteen amino acids subtracted and four amino acids replaced at the weakest points in the peptide structure. Soule et al write that “D-Ala2 substitution contributes to the enhancement of biological activity by reducing metabolic clearance.” [3] In a comparison study with synthetic exogenous GH for treating prepubertal GH deficiency, Lanes and Carillo concluded that “GHRH (1-29) at the dose and schedule used is generally effective in the treatment of GH deficiency.” [4] Campbell et al explain both GHRH(1-44)’s shortcomings in treatment as well as advantages offered by Modified GRF (1-29) and specific structural differences: Native human GRF(1-44)-NH2(hGRF44) is subject to biological inactivation by both enzymatic and chemical routes. In plasma, hGRF44 is rapidly degraded via dipeptidylpeptidase IV (DPP-IV) cleavage between residues Ala2 and Asp3. The hGRF44 is also subject to chemical rearrangement (Asn8-->Asp8, beta-Asp8 via aminosuccinimide formation) and oxidation [Met27-->Met(O)27] in aqueous environments, greatly reducing its bioactivity. It is therefore advantageous to develop long-acting GRF analogues using specific amino acid replacements at the amino-terminus (to prevent enzymatic degradation): residue 8 (to reduce isomerization) and residue 27 (to prevent oxidation). Inclusion of Ala15 substitution (for Gly15), previously demonstrated to enhance receptor binding affinity, would be predicted to improve GRF analogue potency. Substitution of [His1,Val2]-(from the mouse GRF sequence) for [Tyr1,Ala2]-(human sequence) in [Ala15,Leu27]hGRF(1-32)-OH analogues completely inhibited (24-h incubation) DPP-IV cleavage and greatly increased plasma stability in vitro. Additional substitution of Thr8 (mouse GRF sequence), Ser8 (rat GRF sequence), or Gln8 (not naturally occurring) for Asn8 (human GRF sequence) resulted in analogues with enhanced aqueous stability in vitro (i.e., decreased rate of isomerization). These three highly stable and enzymatically resistant hGRF(1-32)-OH analogues, containing His1, Val2, Thr/Gln8, Ala15, and Leu27 replacements, were then bioassay for growth hormone (GH)-releasing activity in vitro (rat pituitary cell culture) and in vivo (SC injection into pigs). Enhanced bioactivity was observed with all three hGRF(1-32)-OH analogues. In vitro, these analogues were approximately threefold more potent than hGRF44, whereas in vivo they were eleven- to thirteen fold more potent.[5] Just as GHRH and Ghrelin work in conjunction through different means for maximal GH release within the body, exogenous GHRH such as Modified GRF (1-29) results in a synergistic effect when used with a Ghrelin mimetic, such as the hexapeptide known as GHRP-6. [6] Pandya et al also conclude that “GHRH is necessary for most of the GH response to GHRP-6 in humans.” [6] Massoud et al conclude that “Hexarelin and GHRH-(1-29)-NH2 are synergistic” [7] (Ed note:Hexarelin is another Ghrelin mimetic). Sawada writes that “findings suggest that the KP-102-induced GH secretion largely depends on GRF and the secretagogue potentiates the GRF effect by antagonizing the SS action at the level of somatotropes. It is concluded that KP-102 alone or in combination with GRF provides a means of stimulating GH secretion in the face of elevated inhibitory tone mediated by SS.” [8] (Ed note: KP-102 is the Ghrelin mimetic GHRP-2) An abstract of a review by Hamilton touches on the main advantage of GRF(1-29) over, for example, CJC-1295 or synthetic GH: …growth hormone secretion occurs in a rhythmic pattern regulated by intricate interactions between two neurohormones: growth hormone-releasing hormone (GHRH) and somatotropin release-inhibiting factor (SRIF).[…] research also indicates that there are sexual differences in the pattern of growth hormone release and that growth hormone regulates its own secretion by means of a negative feedback system. [9] By mimicking natural release patterns with properly dosed and timed GHRPs (Ghrelin mimetics) and GHRH-analogues, negative feedback and undesirable side effects that are typically seen in synthetic GH therapy or even with past forms of GHRH administration (such as constant low-dose administration via pump) can be avoided. For achieving ends other than restoring natural GH release in diseased patients, optimized rhythmic or pulsatile dosing of GHRH with or without a GHRP may be useful, as Vittone et al write about their findings on GHRH applied to healthy elderly men: …data suggest that single nightly doses of GHRH are less effective than multiple daily doses of GHRH in eliciting GH- and/or IGF-I-mediated effects. GHRH treatment may increase muscle strength, and it alters baseline relationships between muscle strength and muscle bioenergetics in a manner consistent with a reduced need for anaerobic metabolism during exercise. Thus, an optimized regimen of GHRH administration might attenuate some of the effects of aging on skeletal muscle function in older persons.

Delta sleep-inducing peptide, abbreviated DSIP, is a neuropeptide that when infused into the mesodiencephalic ventricle of recipient rabbits induces spindle and delta EEG activity and reduced motor activities.Its aminoacid sequence is Тrр-Аlа-Gly-Gly-Asp-Ala-Ser-Gly-Glu. However, it is the only neuropeptide in history whose gene is unknown, raising serious questions regarding the actual existence of this peptide in nature. Delta sleep-inducing peptide was first discovered in 1974 by the Swiss Schoenenberger-Monnier group who isolated it from the cerebral venous blood of rabbits in an induced state of sleep. It was primarily believed to be involved in sleep regulation due to its apparent ability to induce slow-wave sleep in rabbits, but studies on the subject have been contradictory.Delta-sleep-inducing peptide (DSIP)-like material has been found in human breast milk. DSIP is an amphiphilic peptide of molecular weight 850 daltons with the amino acid motif:N-Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu-C It has been found in both free and bound forms in the hypothalamus, limbic system and pituitary as well as various peripheral organs, tissues and body fluids.[5] In the pituitary it co-localises with many peptide and non-peptide mediators such as corticotropin-like intermediate peptide (CLIP), adrenocorticotrophic hormone (ACTH), melanocyte-stimulating hormone (MSH), thyroid-stimulating hormone (TSH) and melanin concentrating hormone (MCH). It is abundant in the gut secretory cells and in the pancreas where it co-localises with glucagon. In the brain its action may be mediated by NMDA receptors. In another study Delta sleep-inducing peptide stimulated Acetyltransferase activity through α1 receptors in rats. It is unknown where DSIP is synthesized. In vitro it has been found to have a low molecular stability with a half life of only 15 minutes due to the action of a specific aminopeptidase-like enzyme. It has been suggested that in the body it complexes with carrier proteins to prevent degradation, or exists as a component of a large precursor molecule, but as yet no structure or gene has been found for this precursor.Evidence supports the current belief that it is regulated by glucocorticoids. Gimble et al. suggest that DSIP interacts with components of the MAPK cascade and is homologous to glucocorticoid-induced leucine zipper (GILZ). GILZ can be induced by Dexamethasone. It prevents Raf-1 activation, which inhibits phosphorylation and activation of ERK.

From the age of 3 months until their natural deaths, female outbred Swiss-derived SHR mice were subcutaneously injected on 5 consecutive days every month with 0.1 ml of normal saline (control) or with 1.0 microg/mouse (approximately 30-40 microg/kg) of tetrapeptide Epitalon (Ala-Glu-Asp-Gly) dissolved in 0.1 ml saline. There were 54 mice in each group. The results of this study show that treatment with Epitalon did not influence food consumption, body weight or mean life span of mice. However, it slowed down the age-related switching-off of estrous function and decreased the frequency of chromosome aberrations in bone marrow cells (by 17.1%, P<0.05). It also increased by 13.3% the life span of the last 10% of the survivors (P<0.01) and by 12.3% the maximum life span in comparison with the control group. We also found that treatment with Epitalon did not influence total spontaneous tumor incidence, but inhibited the development of leukemia (6.0-fold), as compared with the control group. The data obtained suggest a geroprotector activity of Epitalon and the safety of its long-term administration in mice.

Follistatin is part of the inhibin-activin-follistatin axis.

Currently there are three reported isoforms, FS-288, FS-300, and FS-315. Two, FS-288 and FS-315, are known to be created by alternative splicing of the primary mRNA transcript. FS-300 (porcine follistatin) is thought to be the product of posttranslational modification via truncation of the C-terminal domain from the primary amino-acid chain.

Although FS is ubiquitous its highest concentration has been found to be in the female ovary, followed by the skin.

The activin-binding protein follistatin is produced by folliculostellate (FS) cells of the anterior pituitary. FS cells make numerous contacts with the classical endocrine cells of the anterior pituitary including gonadotrophs.

In the tissues activin has a strong role in cellular proliferation, thereby making follistatin the safeguard against uncontrolled cellular proliferation and also allowing it to function as an instrument of cellular differentiation. Both of these roles are vital in tissue rebuilding and repair, and may account for follistatin’s high presence in the skin.

In the blood, activin and follistatin are both known to be involved in the inflammatory response following tissue injury or pathogenic incursion. The source of follistatin in circulating blood plasma has yet to be determined, but due to itsautocrine nature speculation suggests the endothelial cells lining all blood vessels, or the macrophages and monocytesalso circulating within the whole blood, may be sources.

Follistatin is involved in the development of the embryo. It has inhibitory action on bone morphogenic proteins (BMPs); BMPs induce the ectoderm to become epidermal ectoderm. Inhibition of BMPs allows neuroectoderm to arise from ectoderm, a process which eventually forms the neural plate. Other inhibitors involved in this process are noggin and chordin.

Follistatin and BMPs are also known to play a role in folliculogenesis within the ovary. The main role of follistatin in the oestrus/menstrus ovary, so far, appears to be progression of the follicle from early antral to antral/dominant, and importantly the promotion of cellular differentiation of theestrogen producing granulosa cells (GC) of the dominant follicle into the progesterone producing large lutein cells (LLC) of the corpus luteum.

There has never been an adequately large randomized controlled trial to prove definitively that HGH provides significant anti-aging benefits and that there are no significantadverse drug reactions; there have been many small studies which are described below.

Some scientific articles have demonstrated that HGH supplementation does not significantly increase muscle strength or aerobic exercise capacity in healthy individuals.[9]While it is possible that there are some advantages, such as an increase in lean body mass, it is also evident that benefits are being exaggerated by some for commercial gain and ineffective products are being sold to unsuspecting consumers.

Some recent small clinical studies have shown that low-dose GH treatment for elderly patients with GH deficiency changes the body composition by increasing muscle mass, decreasing fat mass, increasing bone density and muscle strength, improves cardiovascular parameters (i.e. decrease of LDL cholesterol), and affects the quality of life without significant side effects. It must be emphasized that these studies were small—only tens of patients – and the results were therefore stated tentatively; in the words of one of the cited sources: “Clearly more studies are needed before GH replacement for the elderly becomes established. Safety issues will require close scrutiny, but the data available so far are sufficiently positive to undertake large multicentre, placebo-controlled trials, particularly looking at endpoints associated with prevention of frailty and loss of independence.”

Copper peptides are naturally occurring small protein fragments that have high affinity to copper ions. In human plasma, the level of GHK-Cu is about 200 µg/ml at age 20. By the age of 60, the level drops to 80 µg/ml. In humans, tripeptide GHK-Cu can promote activation of wound healing, attraction of immune cellsantioxidant and anti-inflammatory effects, stimulation of collagenand glycosaminoglycan synthesis in skin fibroblasts and promotion of blood vessels growth. Recent studies revealed its ability to modulate expression of a large number of human genes, generally reversing gene expression to a healthier state. Synthetic GHK-Cu is used in cosmetics as a reparative and anti-aging ingredient.

Loren Pickart isolated the copper peptide GHK-Cu from human plasma albumin in 1973.Pickart noticed that liver tissue obtained from patients aged 60 to 80 years had an increased level of fibrinogen. However, when liver cells from old patients were incubated in the blood from the younger group, the older cells started functioning in nearly the same way as the younger liver tissue. It turned out that this effect was due to a small peptide factor that behaved similarly to the synthetic peptide glycyl-L-histidyl-L-lysine (GHK). Pickart proposed that this activity in human plasma albumin was a tripeptide glycyl-L-histidyl-L-lysine and that it might function by chelating metal ions.

In 1977, David Schlesinger of the Harvard University Chemistry Department confirmed that the growth modulating peptide isolated by Pickart was a glycyl-L-histidyl-L-lysine peptide.

Further research established that GHK peptide has a strong affinity for copper and exists in two forms – GHK and GHK-Cu. On the basis of the available data, it was proposed that GHK-Cu functions by modulating copper intake into cells.

In the late 1980s, copper peptide GHK-Cu started attracting attention as a promising wound healing agent. Pioneers in this field were J.P Borel and F. Maquart from Université de Reims Champagne-Ardenne (France). At optimal, picomolar to nanomolar concentrations, GHK-Cu stimulated the synthesis of collagen in skin fibroblasts, increased accumulation of total proteins, glycosaminoglycans (in a biphasic curve)and DNA in the dermal wounds in rats. They also found out that the GHK sequence is present in collagen and suggested that the GHK peptide is released after tissue injury.They proposed a class of emergency response molecules which are released from theextracellular matrix at the site of an injury. GHK-Cu also increased synthesis of decorin – a small proteoglycan involved in the regulation of collagen synthesis, wound healing regulation and anti-tumor defense.

The same group established that GHK-Cu stimulated both the synthesis of metalloproteinases, the enzymes which break down dermal proteins, and their inhibitors (anti-proteases). The fact that GHK-Cu not only stimulates the production of dermal components, but also regulates their breakdown suggests that it should be used with caution.

A series of animal experiments established pronounced wound healing activity of copper peptide GHK-Cu. In the dermal wounds of rabbits GHK-Cu facilitated wound healing, causing better wound contraction, faster development of granular tissue and improved angiogenesis. It also elevated the level of antioxidant enzymes.
GHK-Cu has been found to induce a systemic enhancement of healing in rats, mice, and pigs; that is, the GHK-Cu peptide injected in one area of the body (such as the thigh muscles) improved healing at distant body areas (such as the ears). These treatments strongly increased healing parameters such as collagen production, angiogenesis, and wound closure in both wound chambers and full thickness wounds.
Biotinylated GHK-Cu was incorporated into a collagen membrane, which was used as a wound dressing. This GHK-Cu enriched material stimulated wound contraction and cell proliferation, as well as increased expression of antioxidant enzymes. The same material was tested for wound healing in diabetic rats. GHK-Cu treatment resulted in faster wound contraction and epithelization, higher level of glutathione and ascorbic acid, increased synthesis of collagen, and activation of fibroblasts and mast cells. Ischemic open wounds in rats treated with GHK-copper healed faster and had decreased concentration of metalloproteinases 2 and 9 as well as of TNF-beta (a major inflammatory cytokine) compared with vehicle alone or with untreated wounds.


A 2% GHK gel showed promising results in treatment of 120 diabetic patients, increasing the percentage of ulcer closure from 60.8% to 98.5%, and decreasing the percentage of infection from 34% to 7%. The rate of healing was three times greater with GHK.However, a 0.4% GHK-Cu cream failed to reach therapeutic goal in treatment of venous ulcers.


Radioactive anti-cancer treatment slows cell replication by breaking DNA strands. A recent study showed GHK-Cu’s ability to restore function of irradiated fibroblasts to that of intact cells. The researchers used cultured human fibroblasts obtained from cervical skin that was either intact or exposed to radioactive treatment (5000 rad). At a very low (1 nanomolar) concentration, GHK-Cu stimulated irradiated fibroblasts growth and increased their production of growth factors bFGF and VGF to the point where it became even higher than that of both the irradiated and intact control cells.

In 2005, Ahmed et al. demonstrated that GHK promotes nerve regenerationAxon regeneration was studied using collagen tubes with incorporated peptides. GHK increased migration of hematogenous cells into collagen tube, production of nerve growth factors, expression of integrins and the rate of regeneration of myelinated nerve fibers. In addition, GHK also increased axon count and proliferation of Schwann cells compared to the control.


In 2010, Hong Y. et al. demonstrated that GHK-Cu is able to reverse the expression of certain genes involved in metastatic spreading of colon cancer. GHK-Cu was effective at a very low concentration – 1mkM.A 2012 paper reports that GHK, at a very low concentration, does not harm normal fibroblasts (a major repair cell) but did induce programmed cell death two cancer cell lines. Thus, GHK reversed this effect of the cancer cells on the genes.

Recent genomic research suggests that GHK directly modulates gene expression, which may explain the diversity of its biological actions. Iorio et al. used a repository of transcriptional responses to compounds, the Connectivity Map (cMap), and MANTRA software to explore networks of compounds producing similar transcriptional responses. GHK, as one of the compounds studied, increased mRNA production in 268 genes while suppressing 167.GHK was found to reverse the gene-expression signature of emphysematous destruction found in lung tissue obtained from smokers with COPD (Chronic Obstructive Pulmonary Disease). The gene expression signatureassociated with emphysema severity included 127 genes, involved in inflammation and repair. Using the Connectivity Map, researchers established that the peptide GHK downregulated genes involved in lung destruction and inflammation, while upregulating genes involved in tissue repair. Addition of 10 nanomolar GHK to lung fibroblasts from emphysema lungs restored their ability to remodel collagen and assemble it into properly organized fibrils.


Abdulghani et al. established that facial cream containing GHK-Cu increased collagen in photoaged skin of 20 female volunteers, performing better than vitamin C and retinoic acid.

Leyden et al. conducted a 12-week facial study of GHK-Cu containing face and eye cream, reporting significant improvement of skin laxity, clarity and appearance, reduced fine lines and the depths of wrinkles and increased skin density and thickness comparing to placebo. GHK-Cu eye cream performed better than vitamin K cream.

Finkley et al. conducted 12 week facial study on 67 women and reported that GHK-Cu cream applied twice daily improved aged skin appearance, increased thickness, reduced wrinkles and strongly stimulated dermal keratinocyte proliferation as determined by histological analysis of biopsies. The same study found copper peptide GHK-Cu to be non-toxic and non-irritating.


Research of the copper binding properties of GHK and two synthetic peptides, in which histidine was replaced with a synthetic amino acid, established that the amino acidglycine plays major role in copper binding, while lysine can interact with copper only at alkaline pH. At physiological pH, lysine is able to interact with a cellular receptor. The ability of GHK to interact both with copper and with a cellular receptor allows it to transfer copper into and from cells. The small size of GHK permits speedy traveling in extracellular space and its easy access to cellular receptors.

The molecular structure of the GHK copper complex (GHK-Cu) has been extensively studied using X-ray crystallography, EPR spectroscopy, X-ray absorption spectroscopy, NMR spectroscopy as well as other methods such as titration. In the GHK-Cu complex, the Cu (II) ion is coordinated by the nitrogen from the imidazole side chain of the histidine, another nitrogen from the alpha-amino group of glycine and the deprotonated amide nitrogen of the glycine–histidine peptide bond. Since such a structure couldn’t explain a high stability constant of the GHK-Cu complex (log 10 =16.44 vs. 8.68 of the GH copper complex, which is similar to the GHK-Cu structure), it was proposed that another amino group participates in the complex formation. According to the recent study by Hureau et al. the Cu(II) is also coordinated by the oxygen from the carboxyl group of the lysine from the neighboring complex. Another carboxyl group of lysine from a neighboring complex provides the apical oxygen, resulting in the square-planar pyramid configuration. Many researchers proposed that at the physiological pH, GHK-Cu complexes can form binary and ternary structures which may involve amino acid histidine and/or the copper binding region of the albumin molecule. Lau and Sarkar found also that GHK can easily obtain copper 2+ bound to other molecules such as the high affinity copper transport site on plasma albumin ((albumin binding constant log 10 =16.2 vs. GHK binding constant 16 log 10 =16.44). It has been established that copper (II) redox activity is silenced when copper ions are complexed with the GHK tripeptide, which allows the delivery of non-toxic copper into the cell.

Copper is a transition metal that is vital for all eukaryotic organisms from microbes to humans. A dozen enzymes (cuproenzymes) use changes in copper oxidation state to catalyze important biochemical reactions including cellular respiration (cytochrome c oxidase), antioxidant defense (ceruloplasmin, superoxide dismutase (SOD), detoxification (metallothioneins), blood clotting (blood clotting factors V and VIII), melanin production (tyrosinase) and the connective tissue formation (lysyl peroxidase). Copper is required for iron metabolism, oxygenation, neurotransmission, embryonic development and many other essential biological processes. Another function of copper is signaling – for example, stem cells require a certain level of copper in the media to start their differentiation into cells needed for repair. Thus, GHK-Cu’s ability to bind copper and to modulate its tissue level is a key factor determining its biological activity

Growth hormone releasing hexapeptide (GHRP2) is one of several synthetic met-enkephalin analogs that include unnatural D-amino acids, were developed for their growth hormone (GH) releasing activity and are called GH secretagogues. They lack opioid activity but are potent stimulators of GH release. These secretagogues are distinct fromgrowth hormone releasing hormone (GHRH) in that they share no sequence relation and derive their function through action at a completely different receptor. This receptor was originally called the GH secretagogue receptor, but due to subsequent discoveries, the hormone ghrelin is now considered the receptor’s natural endogenous ligand. Therefore, these GH secretagogues act as synthetic ghrelin mimetics.

GHRP-2 secretagogues differ from exogenous rHGH in their effects primarily due to the fact that endogenous GH contains all 5 isoforms of growth hormone, whereas exogenous GH contains only the 20 kilodalton isoform. Different isoforms affect tissues in discreet ways that the 20 kDa isoform cannot. Administration of GH secretagogues causes a pulse-release of GH from the pituitary which is cleared from the body within a few hours. This does not significantly raise plasma IGF1 levels.

Growth hormone (GH) secretion in middle and late adulthood declines with age. However, the precise mechanisms causing this impairment in GH release are unknown. His-D-Trp-Ala-Trp-D-Phe-Lys-NH2 (GHRP-6) is a synthetic compound that releases GH in a dose related and specific manner in several species, including man. In order to gain a further insight into disrupted GH secretion in late adulthood, we evaluated GH responses to GHRP-6 or GHRH, administered either alone or in combination, in healthy young and late adulthood groups of subjects.

These data show that GH responses to GHRP-6 are much greater than to GHRH in late adulthood. The marked increase of plasma GH levels observed after administration of GHRP-6 alone or in combination with GHRH indicates that impaired GH secretion in late adulthood is a functional and potentially reversible state.

Triptorelin, a decapeptide (pGlu-His-Trp-Ser-Tyr-D-Trp-Leu-Arg-Pro-Gly-NH2), is a gonadotropin-releasing hormone agonist(GnRH agonist) used as the acetate or pamoate salts. By causing constant stimulation of the pituitary, it decreases pituitary secretion of gonadotropins luteinizing hormone (LH) and follicle stimulating hormone (FSH). Like other GnRH agonists, triptorelin may be used in the treatment of hormone-responsive cancers such as prostate cancer or breast cancerprecocious puberty,estrogen-dependent conditions (such as endometriosis or uterine fibroids), and in assisted reproduction. It is also used as therapy for gender identity disorder. Triptorelin is marketed under the brand names Decapeptyl (Ipsen) and Diphereline andGonapeptyl (Ferring Pharmaceuticals). In the United States, it is sold by Watson as Trelstar. In Iran Triptorelin is marketed under the brand name Variopeptyl (Varian Darou Pajooh).

During the treatment of prostate cancer it does cause a surge of testosterone (an initial uplevel of testosterone levels), known as a flare effect. In men a reduction of serum testosterone levels into the range normally seen after surgical castration occurs approximately two to four weeks after initiation of therapy. In contrast, gonadotropin-releasing hormone antagonists do not cause a surge, but a sudden reduction of testosterone levels.

Hexarelin is an appetite-regulating factor secreted from peripheral organs that is involved in regulation of energy homoeostasis via binding to the receptor resulting in the secretion of growth hormone by the pituitary gland.  The pathway activated by binding of ghrelin to the growth hormone secretagogue receptor, GHSR1a, regulates the activation of the downstream mitogen-activated protein kinaseAktnitric oxide synthase, and AMPK cascades in different cellular systems.One of the important features of GHSR1a displays constitutive activity possessing basal activity in the absence of an agonist, resulting in a high degree of receptor internalization as well as of signaling activity. Inverse agonists for the ghrelin receptor could be particularly interesting for the treatment of obesity. This activity seems to provide a tonic signal required for the development of normal height, probably through an effect on the GH axis.



IGF-I Des(1-3) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 67 amino acids (aa 4-70) and having a molecular mass of 7372 Dalton.  IGF-1 Des1-3 is purified by proprietary chromatographic techniques.

The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed ‘sulfation factor,’ which later became known as ‘somatomedin’ (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).

BPC 157

You have heard about peptides that boost muscle mass and bone density in patients with muscle wasting diseases. There are other peptides in research labs that are being looking at for their healing properties. BPC 157 is a peptide researchers believe can boost ligament healing in rats. A quick look at BPC 157 explains its properties and uses, as well as its life in the lab.


BPC-157, or PL 14736, is an injectable or oral pentadecapeptide. BPC-157 (body protection compound) is a string of 15 amino acids. Researchers are testing the therapeutic compound on rats to better understand the healing properties of BPC 157, specifically on the ligaments and tissue.


You have heard the term ‘amino acids’ in fitness and nutrition blogs, but what are they and what do amino acids do for the body?

An amino acid is an organic compound that contain carboxyl and amino groups. Amino acids are required for both young children and older adults. Amino acids are building blocks for proteins. There are 20 amino acids, and the body can naturally produce 10 of them. Amino acids in the body are:

  • Asparagine (N)
  • Proline (P)
  • Aspartic acid (D)
  • Cysteine (C)
  • Glutamine (Q)
  • Glycine (G)
  • Serine (S)
  • Alanine (A)
  • Tyrosine (Y)
  • Glutamic acid (E)

The thing about amino acids is your body needs important amino acids for development, but the body can’t produce all the ones it needs on its own. Additional amino acids your body need, that it can’t make on its own, are:

  • Isoleucine (I)
  • Leucine (L)
  • Lysine (K)
  • Methionine (M)
  • Phenylalanine (F)
  • Threonine (T)
  • Tryptophan (W)
  • Valine (V)

As a result, amino acids need to be added to the diet because our bodies cannot store amino acids for future use.


BPC-157 is a string of 15 important amino acids, that is where the name pentadecapeptide comes from. The amino acid structure of BPC-157 is GEPPGKADDAGLV. As you can see, BLC-157 as both essential and nonessential amino acids. Nonessential amino acids are the ones our bodies produce naturally. Essential ones are the acids out bodies need but can’t get on their own. Essential acids must be added to the diet.


Before, I mentioned that amino acids are the building blocks for proteins. When the body breaks down and digests proteins, amino acids are left over to break down food, repair body tissue, aid in bodily functions, and to boost growth.


Early research of BPC-157 in lab mice found that the peptide was effective therapeutic compound for healing damage in gut caused by ulcers.

In 2010, a clinical study on rats found that BPC-157 improved healing of the medial collateral ligament (MCL) up to 90 days after an operation. The therapeutic use of BPC-157 when given orally improved functional, macroscopic, biomechanical and histological healing in the ligament injury. The research team concluded that BPC-157 improves injuries, specifically acute ligament injuries in rats (Cerovecki et al, 2010).[1]

More recently, various studies looked at BPC-157 as a wound healing therapy for healing ulcers in rats.[2]

Read more about the difference between research peptides for sale online.


LGD-4033 is a SARM you might be familiar with if you are a basketball fan. Joakim Noah from the Knicks was suspended when he had to take a drug test. He tested positive for the unapproved substance. Nohan had to sit out 20 games for the therapeutic compound  He is the NBA player who was suspended for 20 games after failing a drug test for having LGD-4033 in his system. What is the SARM LGD-4033 for sale online?


SARMS, or selective androgen receptor modulators, are therapeutic compounds that target the androgen receptor gene in the body. AR, androgen receptor (NR3C4), is a gene that is responsible for binding to androgenic hormones in the body such as  DHT, DHEA and DHEA, or testosterone.

When you think of AR and androgens, men usually come to mind, even if you have never heard the term. Androgens in men are responsible for testosterone. Testosterone is an important hormone in the body that gives men the features of “masculinity.” Testosterone is linked to building muscle, developing sex organs, and developing a male’s libido. AR works a little differently in women. AR is can be converted to female hormones in women. The dominant female hormone in women is estrogen. It is important to understand AR to understand how SARMs like LGD-4033 affect these systems.


LGD-4003 has been studied to specifically target muscles and bones, which avoids the typical side effects commonly associated with testosterone treatments. Clinical studies of LGD-4033 have shown that it has the potential to help improve the growth of lean muscle mass, improve muscle strength, reduce BMI, and to potentially heal tissue and joint damage as the result of certain muscle wasting diseases and age-related conditions.


In 2013, 76 healthy male participants between the ages of 21 and 50 years participated in a research study on LGD-4033. Researchers used the non-steroidal SARM LGD-4033 to analyze not only the safety of the therapeutic compound  but the body’s tolerance to the SARM. The study also observed the SWARM’s ability to target specific muscles and muscle processes.

Researchers conducted pre-clinical trials were done on monkeys over three months. Each group of monkeys was given different doses of LGD-4033. During the study, monkeys gained weight, and after testing the highest dose – 75 mg/kg – research stopped out of fear of toxicity, but the team did not notice adverse outcomes.

For 3 weeks, clinical researchers administered LGD-4033 to the men in the study. The researchers continued to monitor hormone presence, lean mass, fat mass, and muscle strength for up to 5 weeks after the 21-day trial ended. The study concluded that the participants tolerated the SARM LGD-4033 without negative drug-related side effects that are usually seen in testosterone treatments.  Using LGD-4033 over the 3-week period resulted in increases in lean muscle mass in the male participants. The researchers also didn’t notice changes in the prostate antigen. The researchers recommended further studies for future research of LGD-4033 to view the potential benefits of LGD-4033 in specific populations.[1]

Quick overview of the studies benefits of LGD-4033 are:

  • Improved lean muscle mass
  • Greater bone density and strength
  • High tolerability
  • Better results with lower doses than traditional testosterone therapies
  • Results with minimal use and lower dosage


Mk-677, or nutrabol, is a growth hormone secretagogue that has been studied for possible treatments for everything from obesity to muscle wasting diseases. Learn about MK-677, and read the latest research timeline for MK-677 in labs.


To understand what a growth hormone secretagogue (GHS) is, let’s break the term up a little. Secretagogue is a class of drugs that induces secretion. In this case, the secretagogue secrets the growth hormone (GH). GH is an essential hormone in the body produced by the pituitary gland. GH sparks growth when we are kids, and it is essential for maintaining our tissues and muscles as we get older, the pituitary gland doesn’t produce as much GH.

That is where GSHs come in. GSHs are synthetic compounds that can be either non-natural peptidyl or non-peptidyl molecules that influence/stimulate somatotroph (type of acidophil of the adenohypophysis that secretes GH) secretion. Simply, GHSs are man-made compounds that kickstart growth hormone production.

1998 study concluded that taking GHSs orally can increase the production of an insulin-like growth factor (IGF-1)., Additional reported benefits of GHSs include increasing GH in the body (Ghigo et al, 1998)[1], which is beneficial in those with GH deficiencies.


Patients who suffer from a GH deficiency, as well as older adults who experience slowed GH production in the body may experience:

  • Decreased muscle tone and mass
  • Reduced bone mass
  • Decreased muscle strength
  • Delayed puberty
  • Visceral fat and fat around the face
  • Slowed hair growth in children and baldness in men
  • Anxiety
  • Fatigue and sluggishness
  • Low energy levels
  • Skin problems
  • High LDL cholesterol levels (bad cholesterol)
  • Reduced sexual activity and interest

Some people turn to hGH (human growth hormone) to combat low GH levels, but research is also being done on peptidyl compounds (Peptides) such as MK-677 as an alternative as well.


MK-677 is an oral peptidyl compound that is classified as an GHS. Research on MK-677 aims to tackle common problems associated with low GH levels. MK-677 is a compound that is taken orally. It does not require direct injection into the body or a specific muscle.

In 1998, researchers conducted an obesity study. Obesity, it reports, is associated with stunted GH levels in the body, which results in larger body composition and increased risk for cardiovascular diseases. The study observed 24 obese males and the effects MK-677 has on obesity as a result of low levels of GH. The researchers concluded that MK-677 treatments increased GH. The adult males in the study experienced with anabolic effects of MK-677 such as energy expenditure and changes in body composition with a sustained increase in fat-free mass (Svensson et al, 1998).[2] 

A year later, researchers investigating the benefits of MK-677 looked at its relationship to bone turnover in elderly patients. Bone turnover is the total volume of bone that is lost and regained over[3] a certain amount of time. The research on MK-677 found that daily doses of the peptide stimulated bone turnover in elderly patients with age-related bone loss. The team found markers of bone resorption and formation of the course of the 9-week study (Murphy et al, 1999)

In a nutshell, researchers found links between MK-677 and increased bone mass, lower obesity, and improved body composition, all without reporting negative side effects of MK-677.


Hexarelin is a member of the growth hormone family of peptide compounds. Its structure is similar to that of GHRP-6 and it acts as a growth hormone secretagogue to stimulate the growth hormone. Hexarelin causes both the pituitary gland and hypothalamus to react and is responsible for the growth of cells or regeneration of cells.


In numerous laboratory studies of Hexarelin with animal test subjects including mice and rats, when Hexarelin is injected subcutaneously through the top layer of the animal test subject’s skin using a short needle, growth hormone levels significantly increased when the concentration of plasma was measured within thirty minutes of injecting Hexarelin. 

Because Hexarelin increases the natural secretion of growth hormone the effects experienced by animal test subject are very similar to the effects experienced when synthetic GH is used, although to a lesser degree.

Research and laboratory studies report Hexarelin injection effects to include:

  • Increased strength
  • Increased growth of new muscle
  • Increased size of existing muscle
  • Increased bone density
  • Decreased body fat
  • Rejuvenation of joints
  • Neural protection
  • Improved elasticity of skin
  • Improved ability to heal after injury

When there is an increase in growth hormone the levels of Insulin-Like Growth Facor (IGF-1) increase within the liver. The increase of IGF-1 contributes to muscle growth when growth hormone is stimulated.


IGF-1 has a similar molecular structure as insulin. It is a protein consisting of 70 amino acids in a single chain. It offers anabolic effects. In test subjects, Synthetic IGF-1, called mecasermin, was shown as a possibility for treating growth failure.

Normally, testing has shown that increasing growth hormone will lead to an increase in appetitite. Testing of Hexarelin did not show this side effect and it is thought to be because Hexarelin does not increase Ghrelin levels to the same degree that GHRP-6 does, and so it does not increase hunger or result in quicker gastric emptying.


After the animal test subject receives a cycle of Hexarelin for research purposes, side effects are noted. The side effects are not severe or long lasting, but include:

  • Increased prolactin levels
  • Increased cortisol
  • Decreased libido
  • Potential for gynecomastia


Hexarelin creates similar reactions as GHRP-6, in that test subjects have an increase of growth hormone circulated through their bodies. What makes it unique is that it acts on cardiac receptors separately from the ability to release and increase growth hormone. Hexarelin is being studied for the potential of using the compound to assist in cardio pressure issues and healing heart scar tissue. Cardio protective properties were experienced by both lean and obese lab rats, while the growth hormone plasma increase was not fully experienced by obese lab rats.  The healthier the lab test subject was prior to receiving Hexarelin, the more efficiently it produced and used the growth hormone.


MGF is a compound used for research purposes to understand its involvement in tissue repair and regeneration in studies conducted with rodents.


MGF, also known as Mechano Growth Factor and 1GF-IEa, is a variant of the IGF (insulin-like growth factor) gene. IGFs are proteins in the body that have have high sequence parallels similar to insulin. MGF is a splice variant of the proteins that is thought to boost stem cell production in muscle and tissues.

When splicing of the IGF-1 gene occurs, it does so early in the skeletal muscle response to either surgical resection of a tendon or electrical stimuli. As a result, a distinct peptide is generated that is distinctive of the typical 70-amino-acid IGF-1 peptide. The distinct peptide is MGF, and companies now produce synthetic versions may improved precursor cell proliferation. 

What that means is the increase or production of precursor cells increases the number of cells.

In the liver, 2 different types of MGF splices occur:

  1. First phase release: IGF-1Ec that stimulates satellite cells. It has anabolic properties that are similar to synthetic versions of MGF created in the lab for research purposes.
  2. Second phase of release: The less anabolic splice variant is IGF-1Ea

Research on MGF is directed at MGF’s ability to activate muscle and tissue stem cells and boosting protein synthesis to prevent and repair wasted tissue cells after injury. To improve muscle mass and cell health overtime, MGF can signal satellite cell activation and increase protein synthesis.

The nature of MGF makes is a desired synthetic for research purposes. Expression of MGF is responsible for repairing and regenerating tissues by activating satellite cells (Zhang et al, 2012). In study with mice, researchers discovered overexpression of MGF in mice brains increases proliferating cells. The overexpression of MGF increases neural progenitor cells and boosts neurogenesis in the brains of aging mice. Neurogenesis is the creation and development of nervous tissues (Tang et al, 2017).

In another study on rodents, researchers uncovered similar evidence that MGF peptide increases both proliferation and satellite cell activation. Results in mice include proliferation and fusion to promote muscle repair and maintenance, which are important factors for combating muscle loss due to aging (Kandalla et al, 2011).


When cells are damaged as the result of use and hypertrophy, two forms of the MGF splice variant occur. The process requires MGF to preserve the cells and prevent cell death. When used in research studies, specifically on rats, MGF is injected directly into the muscle to replenish MGF to increase recovery and stimulate new cell growth. Intramuscular injections of MGF in rodents should occur within the first 5 minutes of trauma and hypertrophy.

Because of its anabolic properties, researchers are exploring the uses of MGF for treating the effects associated with muscle wasting diseases in aging. Researchers have observed the effectiveness of bilateral use of 200mcg in affected areas. Typically, research on MGF spans 4-week-long trials between cycles to improve cell recovery and reproduction, dosing up to three times per week. Research on MGF shows results when using MGF for a total of 6 months.


A Growth Hormone Releasing Hormone (GHRH) peptide analogue, Sermorelin Acetate, is also known as GRF 1-29. It is commonly mistaken for Human Growth Hormone (HGH) but it is not the same thing. It was once listed under the trade names of Geref and Gerel but has been discontinued. The GHRH is released by the brain and responsible for stimulating the release of Growth Hormone (GH) by the pituitary gland. Sermorelin is a synthetic peptide that contains 29 amino acids and has the following sequence and molecular formula:

Sequence: H-Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-NH2

Molecular formula: C149H246N44O42S

Sermorelin is considered to be a growth hormone secretagogue because it offers the function of GHRH and has the shortest synthetic peptide sequence with just 29 amino acids.  GHRH has 44 amino acids, and is called a polypeptide. It’s naturally produced in the periventricular arcuate neuron cell bodies.


The Growth Hormone promotes healthy, efficient metabolisms. When GHRH stimulates growth hormone, it’s also been shown that it can produce non-rapid eye movement sleep. If an individual does not have enough GHRH, they may suffer from insomnia or other sleep disorders that prevent an individual from waking up feeling rested.


During clinical studies, Sermorelin has been used to stimulate secretion of the growth hormone from the anterior pituitary, and to assess for pituitary sufficiency in its ability to secrete the growth hormone. Scientists first began studying GHRH in the 1980s, originally for its potential to be used as a tool in the anti-aging process and for use as an alternative to growth hormone replacement therapies.

In 1999, a Sermorelin study was published in the journal, Biodrugs. It was an investigation of whether or not an injection of Sermorelin would stimulate Growth Hormone secretion from the anterior pituitary. Test subjects were divided into two groups with one group receiving subcutaneous injections while the other group received Sermorelin intravenously. Both groups presented the same result, in that Sermorelin can diagnose a Growth Hormone insufficiency in people affected by Growth Hormone deficiencies and that it can accelerate growth.

Clinical studies show that Sermorelin therapy increases the amount of the hormone the pituitary gland secretes, and once released in the body it is later converted to IGF-1 by the liver – increasing the body’s ability to grow new cells in the organs and bones, and increasing metabolism.


Lipopeptide has a few different uses. Lipopeptides are a research chemical desired for collagen production and improving HA (hyaluronic acid) productivity. Human use of the peptide Lipopeptide is forbidden. Lipopeptide is used for research purposes only.


The three-letter code for lipopeptide is Pal-Gly-Gln-Pro-Arg-OH.

Lipopeptide is a molecule with a lipid and peptide attached to each other. TLR 1 and other toll-like receptors create the bond. Toll-like receptors are important proteins that plan a significant role in the body’s immune system. TLRs are essential for the initial invasion of pathogens in the body. TLRs recognize and the invading microorganisms and assist in defending against them.

The cosmetic lipopeptide is also referred to as biopeptide EL. It is expressed by the presence of bacteria.

Lipopeptide is an interesting molecule because it has the ability to rearrange themselves into different configurations.


In scientific studies, researchers found that lipopeptide is uniquely situated to increase cell production naturally. It is not a water-soluble peptide, which means it has high bioavailability properties that make it biocompatible on the surface.

Lipopeptides interact directly with cell membranes to boost activity, repair, and reproduce. Each variation has a unique use.

The three types of lipopeptides are: bacterially-expressed lipopeptides used as antimicrobial and antifungal use; linear toll-like lipopeptides used in immunology and other medical therapies; bio-derived linear lipopeptides that with collagen-stimulating activity that are used in cosmetics. The different structure can be used for different reasons.

The most common reasons for lipopeptide use and research are:

  • Study the increase in natural collagen and hyaluronic acid bioavailability
  • Cell membrane interaction for renewal and regrowth
  • To control plant disease
  • Antifungal

Obviously the lipopeptides used are not the same for each individual use.


Cosmetic use of lipopeptide is done only for research purposes. Human and animal use of lipoptide is prohibited. Research on lipopeptide as an antifungal includes three lipopeptides: fengycin, surfactin, and iturin.

They are antibiotics that were approved by the FDA in 2003 for use on farms for its antifungal and antibacterial properties.

Pharmaceutical and biomedical research on lipopeptides as biosurfactants is used for its antimicrobial, anti-adhesive, antitumor, and anti-mycoplasma properties. Researchers study lipopeptides as therapeutic, probiotic and pharmaceutical agents. In 2008, researchers discovered the antimicrobial potential of lipopeptides from marine microorganisms (Das et al, 2008).

Biomedical research discovered that the antimicrobial and anti-adhesive properties of biosurfactants may be used in protecting processes from microorganisms that cause skin diseases, making it a safer alternative to traditional antibiotics (Gudina et al, 2010).

Lipopeptides used for cosmetic purposes are commercially available lipopeptides that are commercially available. Lipopeptide for cosmetic research is suggested as anti-wrinkle activity. This specific research peptide focuses on the pro-collagen sequences that allow the cells to increase the presence of collagen (Robinson et al, 2005).


When studying the antimicrobial and biocompatibility of lipopeptide, the common dosage is 10 mg. Common lipopeptide studies for biocompatible use also use 200 mg of lipopeptide (Biopeptide EL).


ACE-083 is a locally active agent being researched by Acceleron in their neuromuscular therapeutic program. Acceleron is a research organization focused on the researching of TGF-beta protein superfamily of substances looking to discover and develop medicines that will improve the lives of patients experiencing a wide range of rare or serious diseases. The potential medications researched by Acceleron go through many clinical research trials to see whether or not they could be used to treat patients with unmet medical needs.

ACE-083 is being studied for its potential to treat muscle loss such as that which occurs with muscular dystrophies. The belief is that ACE-083 would increase strength and overall functioning of specific muscles to improve the quality of life of patients experiencing muscle loss or neuromuscular disease symptoms.


Acceleron is studying the effects of using multiple TGF-beta targets in clinical research to increase strength and muscle mass in the muscle where the substance is administered. Research has shown that ACE-083 achieves results by preventing select proteins in the TGF-beta protein superfamily from reducing the growth of muscle. For example, myostatin (GFF8) works to stop the production of muscle, so if ACE-083 can prevent myostatin from activating, then muscle will continue to grow. During research trials, it’s also been discovered that ACE-083 does not affect untreated muscles or any other organs beyond the site of administering the injection. This reduces the potential for systemic side effects.


Healthy volunteers work with Acceleron to test results of using ACE-083. In Phase 1 trials, research shows measurable increases in muscle volume as a result of administration of ACE-083. The amount of muscle volume was directly related to the dose of ACE-083.

Results from Phase 1 trials lead to a two-par Phase 2 trial in test subjects experiencing muscle weakness in their biceps or tibialis anterior and a separate trial of test subjects suffering from reduced mobility and foot drop as a result of muscle weakness.


Individuals with FSHD, the most common of muscular dystrophies, experience trouble walking, running, and using their upper arm muscles. The disease affects 20,000 in the United States and eventually limits their ability to perform daily tasks most people take for granted, such as getting dressed or preparing a meal. Roughly 20% of people with FSHD will eventually require a wheelchair. At this time, there are no FDA-approved treatments or therapies. Treatment currently involves surgical methods or physical therapy.

Acceleron is hoping ACE-083 will become a potential treatment for FSHD, and much of the research on ACE-083 is for this purpose.


Other clinical research is to determine whether or not ACE-083 can be used to successfully treat Charcot-Marie-Tooth-Disease, an inherited neurological disorder that affects over 100,000 individuals in the United States. Individuals with the disease experience frequent falls as their lower leg muscles lose strength. As the disease progresses, they may also experience muscle atrophy in the feet and hands. With no FDA-approved treatments beyond physical therapy, surgery, or orthopedic equipment, Acceleron is researching ACE-083 to determine if it can become a medication for the disease.


BPC 157, Body Protection Compound 157, also known as PL-10, PL 14736, or Bepecin, is a synthetic substance. Synthetic substances are things that do not occur naturally and are man-made. The BPC 157 formula is a patented supplement created from a protective protein found in human gastric juice. The peptide chain for BPC-157 consists of 15 amino acids, and acts as a signaling peptide in that it signals the body to start certain processes.

BPC is a pentadecapeptide tested in animal trials for its potential for wound healing and cytoprotective activities. Cytoprotection is the process of protecting cells against harmful agents with chemical compounds. For example, a medication that combats the affects of ulcers is a gastric cytoprotectant.


To study the effects of BPC 157 on rats, a dose of the peptide is injected rather than giving the substance orally – because when taken orally, the peptide is poorly absorbed.


Many researchers have used BPC-157 in studies involving rodents. When BPC-157 is administered to rats along with a damaging surgical procedure or a research toxin, the BPC 157 has shown to make protective efforts against stomach ulcers, inflammatory disorders, organ damages, intestinal damage, and bone and joint healing and growth rates. Some studies have indicated the possibility of BPC-157 working to influence growth factors in the production of blood vessels or regeneration after damage, called angiogenesis, but additional research needs to take place to confirm. It is thought that BPC 157 helps form small blood vessels and connective tissue when the body is healing from a wound. BPC 157 also assisted greatly with the survival of the cells after a trauma resulting in a wound.


Research on lab rats have determined the anti-inflammation properties of the BPC 157 peptide make it a potential solution for treating several issues affecting the gastrointestinal tract. Some lab rat studies indicated BPC 157 is effective in treating:

  • Inflammatory bowel disease
  • Ulcerative colitis
  • Collagenous colitis
  • Crohn’s disease
  • Esophagitis


Additional research studies performed on animal test subjects show BPC 157 as a potential treatment for periodontal disease affecting gums and tissues surrounding teeth. BPC 157 reduced the fluid leaking from the gums when an area of the mouth was infected and inflamed. In the studies, healthy tissues and gums in the mouth were completely unaffected by BPC 157.


Various studies have shown BPC 157 affects lab rats in the following ways:

  • For rats with low blood pressure, BPC 157 will increase it.
  • For rats with high blood pressure, BPC 157 will decrease blood pressure.
  • Rats experiencing heart failure, peptic ulcers, or heart failure from a calcium overdose are protected from organ damage when given BPC 157.
  • BPC 157 protected rats in the studies from calcium channel blocker overdose.
  • Rats using BPC 157 were protected from magnesium overdose.
  • Mice given BPC 157 had decreased tolerance to diazepam, physical dependence, and withdrawal symptoms
  • Rats with carcinoma and melanoma B-16 cancers experienced a prolonged life from 25 days to 45 days or more after receiving BPC 157.
  • Withdrawal symptoms in morphine-addicted mice are reduced when they’re given BPC 157


ACVR2B goes by multiple names, including ACE-031, ActRIIB-IgG1, and Activin receptor type-2B. It was originally created and developed by two bio-pharmaceutical companies, Shire and Acceleron, for the possibility of inhibiting myostatin and other proteins which limit muscle growth. The protein is synthetically produced, meaning it does not occur or develop naturally. Many studies have been conducted since the synthetic proteins creation to determine whether or not ACVR2B could be used as an effective treatment of Duchenne Muscular Dystrophy (DMD). Scientific hypothesis of ACVR2B indicate that it would act as a receptor for catabolic proteins like myostatin, as a decoy that would keep the catabolic proteins away from muscle fibers, and as a result – encourage greater muscle growth.

Understanding ACVR2B also requires that you know what Myostatin is and does. 


Myostatin, also known as Growth Differentiation Factor-8 (GDF-8), is a protein that mammals produce in their body. The protein was first discovered by geneticists in 1997 who produced mutant mice that lack the gene that encodes myostatin. As a result, the mutant mice had two times as much muscle as mice with the gene. Myostatin inhibits the process of myogenesis, which is the differentiation and growth of muscle cells.

What does that mean in simple terms? Myostatin tells the cells in the muscles not to grow. When myostatin is blocked, the muscles get bigger.


Scientists and researchers study the ACVR2B bio-peptide for its potential to treat a variety of health conditions and diseases ranging from cancer to cardiovascular abnormalities, to metabolic diseases, to muscular damage and neuromuscular disease. Studies show that ACVR2B stops cells from signaling processes by blocking the ActRIIB receptor which increases muscle power. ActRIIB is basically the switch that turns muscle growth on and off. Using recombinant technology, proteins can be fused to eliminate myostatin, which allows more muscle growth and strength such as was shown in the studies of mutant mice that were missing myostatin.

Researchers working with ACVR2B must take proper precautions to protect themselves during studies. If an of the researchers are exposed to the protein, they are instructed to thoroughly wash it off to avoid adverse reactions.


To test whether or not ACVR2B could be useful in preventing myostatin from putting a halt to muscle growth, researchers have to do the following:

1)Obtain a portion of human DNA containing the tip of a myostatin receptor.

2)Add genetic code to ensure digestive enzymes would cut at the right location on the synthesized DNA and amplify the gene fragment with a polymerase chain reaction.

3) Attach the tip of the myostatin receptor gene to an antibody backbone and splice DNA from a bacteria into place.

4) The bacteria infects the host (test subject) with the new DNA. Antibodies are then produced to bind to myostatin.

5) The newly produced vector is injected into a hamster’s ovary cells.

6) Using a column engineered by GE, the hamster serum is filtered and pulled out of the hamster cell serum. The purified antibodies are called ACVR2B.

7) ACVR2B are injected into male mice to study the effects on muscle fiber.


Adrafanil is a synthetic nootropic, meaning it is a supplement that creates effects on the brain including improved focus, cognition, and a feeling of overall well being. It is a central nervous system stimulant and a precursor drug to modafinil, which means when Adrafanil is used the liver metabolizes it and produces modafinil. Structurally, Adrafanil and modafinil are very similar. The main structural difference between the two substances is that the terminal amide hydroxyl group of adrafinil is lacking in modafinil.

Both modafinil and Adrafanil are stimulants, although Adrafanil reportedly does not cause hyperactivity when ingested, it simply fights the feeling of sleepiness. It is recommended that it is not taken at any time other than first thing in the morning as it has a tendency to prevent sleep as such, it is classified as a eugregorid agent to promote alertfulness and wakefulness.

Adrafinil was discovered first in the 1970’s by pharmaceutical company, Group Lafon, in France.


Adrafanil is also known as CRL-40028, Olmifon, and ({diphenylmethyl}sulfinyl-2 acetohydroxamic acid).

Molecular Formula: C15H15NO3S

CAS ID: 63547-13-7


Like modafinil, Adrafanil is banned by the World Anti-Doping Agency as a nonspecific stimulate compound under section 6 of the 2014 banned substances list. Professional athletes cannot use Adrafanil.

In the United States, Adrafinil is legal to buy and use but it is unregulated by the Food and Drug Administration (FDA). It has not currently been submitted for clinical uses that would require a prescription. In the UK, Adrafinil is also legal to buy and use.


Rats are often used in the studies of Adrafanil. It is found that seven hours after an oral dose is given, it is still detectable in serum. The half-life is determined to be around five hours.

In a study of canines with Adrafinil, it was found that after ten hours the serum Adrafinil levels associated with a high dose is lower than when given a lower dose treatment. Scientists reason that high doses of Adrafinil could induce elimination or metabolism of Adrafinil more so than lower doses.

In another study involving quaking mice, it was found that the mechanism of Adrafinil appears to rely on postsynaptic α-adrenergic activity. Locomotion increases caused by Adrafinil is blocked by prazosin, yohimbine, or phenoxybenzamine.

Increased wakefulness was tested on monkeys at night. After a 60 mg/kg dose, monkeys experienced double activity whereas after the second dose, monkeys quadrupled their locomotion activity.  Rat testing confirms that Adrafinil effects have greater efficacy during periods when the animals would normally be asleep.

In a study of beagle dogs, Adrafinil improved their learning abilities when compared against a placebo group of beagle dogs.



IGF-1 is produced primarily by the liver as an endocrine hormone as well as in target tissues in a paracrine/autocrine fashion. Production is stimulated by growth hormone (GH) and can be retarded by undernutrition, growth hormone insensitivity, lack of growth hormone receptors, or failures of the downstream signalling pathway post GH receptor including SHP2 and STAT5B. Approximately 98% of IGF-1 is always bound to one of 6 binding proteins (IGF-BP).IGFBP-3, the most abundant protein, accounts for 80% of all IGF binding. IGF-1 binds to IGFBP-3 in a 1:1 molar ratio.


In rat experiments the amount of IGF-1 mRNA in the liver was positively associated with dietary casein and negatively associated with a protein-free diet.


Recently, an efficient plant expression system was developed to produce biologically active recombinant human IGF-I (rhIGF-I) in transgenic rice grains.

Its primary action is mediated by binding to its specific receptor, the insulin-like growth factor 1 receptor (IGF1R), which is present on many cell types in many tissues. Binding to the IGF1R, a receptor tyrosine kinase, initiates intracellular signaling; IGF-1 is one of the most potent natural activators of the AKT signaling pathway, a stimulator of cell growth and proliferation, and a potent inhibitor of programmed cell death .[citation needed]

IGF-1 is a primary mediator of the effects of growth hormone (GH). Growth hormone is made in the anterior pituitarygland, is released into the blood stream, and then stimulates the liver to produce IGF-1. IGF-1 then stimulates systemic body growth, and has growth-promoting effects on almost every cell in the body, especially skeletal musclecartilage,boneliverkidneynervesskinhematopoietic cell, and lungs. In addition to the insulin-like effects, IGF-1 can also regulate cell growth and development, especially in nerve cells, as well as cellular DNA synthesis.

Deficiency of either growth hormone or IGF-1 therefore results in diminished stature. GH-deficient children are givenrecombinant GH to increase their size. IGF-1 deficient humans, who are categorized as having Laron syndrome, or Laron’s dwarfism, are treated with recombinant IGF-1. In beef cattle, circulating IGF-1 concentrations are related to reproductive performance.

Insulin-like growth factor 1 receptor (IGF-1R) and other tyrosine kinase growth factor receptors signal through multiple pathways. A key pathway is regulated by phosphatidylinositol-3 kinase (PI3K) and its downstream partner, the mammalian target of rapamycin (mTOR). Rapamycins complex with FKBPP12 to inhibit the mTORC1 complex. mTORC2 remains unaffected and responds by upregulating Akt, driving signals through the inhibited mTORC1. Phosphorylation of eukaryotic initiation factor 4e (eif-4E) [4EBP] by mTOR inhibits the capacity of 4EBP to inhibit eif-4E and slow metabolism.


Insulin-like growth factor 2, also called somatomedin C, is a protein that in humans is encoded by the IGF1gene.IGF-2 has also been referred to as a “sulfation factor”[3] and its effects were termed “nonsuppressible insulin-like activity” (NSILA) in the 1970s.

IGF-1 is a hormone similar in molecular structure to insulin. It plays an important role in childhood growth and continues to have anabolic effects in adults. A synthetic analog of IGF-1, mecasermin, is used for the treatment of growth failure.

IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 has a molecular weight of 7,649 daltons.

Its primary action is mediated by binding to its specific receptor, the insulin-like growth factor 1 receptor (IGF1R), which is present on many cell types in many tissues. Binding to the IGF1R, a receptor tyrosine kinase, initiates intracellular signaling; IGF-1 is one of the most potent natural activators of the AKT signaling pathway, a stimulator of cell growth and proliferation, and a potent inhibitor of programmed cell death .[citation needed] IGF-1 binds to at least two cell surface receptors: the IGF-1 receptor (IGF1R), and the insulin receptor. The IGF-1 receptor seems to be the “physiologic” receptor – it binds IGF-1 at significantly higher affinity than the IGF-1 that is bound to the insulin receptor. Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase – meaning it signals by causing the addition of a phosphate molecule on particular tyrosines. IGF-1 activates the insulin receptor at approximately 0.1 times the potency of insulin. Part of this signaling may be via IGF1R/Insulin Receptor heterodimers (the reason for the confusion is that binding studies show that IGF1 binds the insulin receptor 100-fold less well than insulin, yet that does not correlate with the actual potency of IGF1 in vivo at inducing phosphorylation of the insulin receptor, and hypoglycemia).[citation needed]

IGF-1 is a primary mediator of the effects of growth hormone (GH). Growth hormone is made in the anterior pituitary gland, is released into the blood stream, and then stimulates the liver to produce IGF-1. IGF-1 then stimulates systemic body growth, and has growth-promoting effects on almost every cell in the body, especially skeletal musclecartilageboneliverkidneynervesskinhematopoietic cell, and lungs. In addition to the insulin-like effects, IGF-1 can also regulate cell growth and development, especially in nerve cells, as well as cellular DNAsynthesis.[citation needed]

Insulin-like growth factor 1 receptor (IGF-1R) and other tyrosine kinase growth factor receptors signal through multiple pathways. A key pathway is regulated by phosphatidylinositol-3 kinase (PI3K) and its downstream partner, the mammalian target of rapamycin (mTOR). Rapamycins complex with FKBPP12 to inhibit the mTORC1 complex. mTORC2 remains unaffected and responds by upregulating Akt, driving signals through the inhibited mTORC1. Phosphorylation of eukaryotic initiation factor 4e (eif-4E) [4EBP] by mTOR inhibits the capacity of 4EBP to inhibit eif-4E and slow metabolism.[citation needed]

Insulin-like growth factor 1 has been shown to bind and interact with all the IGF-1 binding proteins (IGFBPs), of which there are seven:IGFBP1IGFBP2IGFBP3IGFBP4IGFBP5IGFBP6, and IGFBP7.[citation needed] Some IGFBPs are inhibitory. For example, both IGFBP-2and IGFBP-5 bind IGF-1 at a higher affinity than it binds its receptor. Therefore, increases in serum levels of these two IGFBPs result in a decrease in IGF-1 activity

Ipamorelin is a new and potent synthetic pentapeptide which has distinct and specific growth hormone (GH)-releasing properties. With the objective of investigating the effects on longitudinal bone growth rate (LGR), body weight (BW), and GH release, ipamorelin in different doses (0, 18, 90 and 450 microg/day) was injected s.c. three times daily for 15 days to adult female rats. After intravital tetracycline labelling on days 0, 6, and 13, LGR was determined by measuring the distance between the respective fluorescent bands in the proximal tibia metaphysis. Ipamorelin dose-dependently increased LGR from 42 microm/day in the vehicle group to 44, 50, and 52 microm/day in the treatment groups (P<0.0001). There was also a pronounced and dose-dependent effect on BW gain. The treatment did not affect total IGF-I levels, IGFBPs, or serum markers of bone formation and resorption. The number of tartrate-resistant acid phosphatase-positive multinuclear cells in the metaphysis of the tibia did not change significantly with treatment. The responsiveness of the pituitary to a provocative i.v. dose of ipamorelin or GHRH showed that the plasma GH response was marginally reduced (P<0.03) after ipamorelin, but unchanged after GHRH. The pituitary GH content was unchanged by ipamorelin treatment. Whether ipamorelin or other GH secretagogues may have a place in the treatment of children with growth retardation requires demonstration in future clinical studies.

lipopeptide is a molecule consisting of a lipid connected to a peptideBacteria express these molecules. They are bound by TLR 1, and other, Toll-like receptors.
Certain lipopeptides are used as antibiotics

TLR 1 is a member of the Toll-like receptor family (TLR) of pattern recognition receptors of the innate immune system.TLR1 recognizes pathogen-associated molecular pattern with a specificity for gram-positive bacteria. TLR1 has also been designated as CD281 (cluster of differentiation 281).

TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognizepathogen-associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production ofcytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. This gene is ubiquitously expressed, and at higher levels than other TLR genes. Different length transcripts presumably resulting from use of alternative polyadenylation site, and/or from alternative splicing, have been noted for this gene.

TLR1 recognises peptidoglycan and (triacyl) lipoproteins in concert with TLR2 (as a heterodimer). It is found on the surface of macrophages and neutrophils.

MGF (mechano growth factor) has been used by bodybuilders and athletes for a few years already. After resistance exercise, IGF-1 is released within the muscle. Specifically, at this time, immediately following the mechanical use of a muscle, the IGF-I gene is spliced towards MGF which initiates hypertrophy and repair of local muscle damage. It does so both by activating muscle stem cells and satellite cells, but also via various other anabolic processes. It differs from “regular” IGF-1 mainly due to it’s C-Terminal sequence.


It was first discovered in the muscle by Goldspink, et al. In human muscle, a 49-base insert changes the reading frame in mechano growth factor (MGF) as compared to IGF-1.

When mechanical overload is introduced to a muscle (as by weight training), the IGF-1 gene released and is differentially spliced during the bodies response. Initially, it it is spliced to produce predominantly IGF-1Ec (called the MGF splice variant of IGF-1). This early splicing stimulates satellite cells into activation. Which in turn allows the activation of extra undamaged nuclei to grow new muscle fiber and tissue. The appearance of MGF also initiates the upregulation of new protein synthesis. After this initial splicing of IGF-1 into MGF, production then switches towards producing a systemic release of IGF-1Ea from the liver, which also upregulates protein synthesis as well. The expression of IGF-1 splice variants, over the course of the healing and regrowth phase of muscle repair is thought to be the primary anabolic mechanism by which the body produces new muscle. MGF is available as an injectable peptide, and it has been anecdotally shown that injecting it will cause a response in the area resulting in localized muscle growth.

Myostatin (also known as growth differentiation factor 8, abbreviated GDF-8) is a protein that in humans is encoded by the MSTN gene.[1] Myostatin is a secreted growth differentiation factor that is a member of the TGF beta protein family that inhibits muscle differentiation and growth in the process known as myogenesis. Myostatin is produced primarily in skeletal muscle cells, circulates in the blood and acts on muscle tissue, by binding a cell-bound receptor called the activin type II receptor.[2][3]

Animals lacking myostatin or animals treated with substances that block the activity of myostatin have significantly larger muscles. This could be of economic benefit to the livestock industry. However these animals require special care and feeding which offsets the potential economic advantage.

Mutations in both copies of the human myostatin gene results in individuals that have significantly more muscle mass and hence are considerably stronger than normal. Furthermore, blocking the activity of myostatin may have therapeutic application in treating muscle wasting diseases such as muscular dystrophy.

The gene encoding myostatin was discovered in 1997 by geneticists Dr. Se-Jin Lee and Alexandra McPherron who also produced a strain of mutant mice that lack the gene. These myostatin “knockout” mice have approximately twice as much muscle as normal mice. These mice were subsequently named “mighty mice”.

Naturally occurring lacks of myostatin have been identified in cattle, whippets, and humans; in each case the result is a dramatic increase in muscle mass. A mutation in the 3′ UTRof the myostatin gene in Texel sheep creates target sites for the microRNAs miR-1 and miR-206. This is likely to cause the muscular phenotype of this breed of sheep.

Buy Myostatin 1mg from Progen Peptide NOW

Oxytocin (/ˌɒksɨˈtsɪn/Oxt) is a mammalian neurohypophysial hormone. Produced by the hypothalamus and stored and secreted by the posterior pituitary gland, oxytocin acts primarily as a neuromodulator in the brain.

Oxytocin plays an important role in the neuroanatomy of intimacy, specifically in sexual reproduction of both sexes, in particular during and after childbirth; its name, meaning “swift childbirth”, comes from Greek ὀξύς, oksys “swift” and τόκος, tokos “birth.” It is released in large amounts after distension of the cervix and uterus during labor, facilitating birthmaternal bonding, and, after stimulation of thenippleslactation. Both childbirth and milk ejection result from positive feedback mechanisms.

Recent studies have begun to investigate oxytocin’s role in various behaviors, including orgasmsocial recognitionpair bonding,anxiety, and maternal behaviors.For this reason, it is sometimes referred to as the “bonding hormone”. There is some evidence that oxytocin promotes ethnocentric behavior, incorporating the trust and empathy of in-groups with their suspicion and rejection of outsiders.Furthermore, genetic differences in the oxytocin receptor gene (OXTR) have been associated with maladaptive social traits such as aggressive behaviour.

Injected oxytocin analogues are used for labor induction and to support labor in case of difficult parturition. It has largely replacedergometrine as the principal agent to increase uterine tone in acute postpartum hemorrhage. Oxytocin is also used in veterinary medicine to facilitate birth and to stimulate milk release. The tocolyticagent atosiban (Tractocile) acts as an antagonist of oxytocin receptors; this drug is registered in many countries to suppress premature labor between 24 and 33 weeks of gestation. It has fewer side effects than drugs previously used for this purpose (ritodrinesalbutamol, and terbutaline).

Pegylated Mechano Growth Factor is a Research Peptide Hormone Mechano Growth Factor adds pegylation process to amino acid peptides synthesis is an original interlaced variant of IGF-1 (Insulin Like Growth Factor-I). MGF is a splice variant of the IGF gene which increases stem cell count in the muscle and allows for muscle fibers to fuse and mature. This is a process required for growth of adult muscle.

Mechano Growth Factor (MGF) also known as IGF-1Ec is a growth factor/repair factor that is derived from exercised or damaged muscle tissue, Its called MGF as IGF-1Ec is a bit of a mouthful and harder to identify amongst the other igf variants.
What makes MGF special is its unique role in muscle growth.
MGF has the ability to cause wasted tissue to grow and improve itself by activating muscle stem cells and increasing the upregulation of protein synthesis, this unique ability can rapidly improve recovery and speed up muscle growth.
MGF can initiate muscle satellite (stem) cell activation in addition to its IGF-Ireceptor domain which ithen in turn ncreases protein synthesis turnover, and therefore can if used correctly improve muscle mass over time.
The liver produces 2 kinds of MGF splice variants of igf..
1) IGF-1Ec This is the first phase release igf splice variant and it appears to stimulate satellite cells into activation, This is the closest variant to synthetic MGF.

2) liver type IGF-IEa this is the secondary release of igf from the liver, and its far less anabolic.

MGF differs from the second variant IGF-IEa as it has a different peptide sequence which is responsible for replenishing the satellite cells in skeletal muscle, in other words it is more anabolic and longer acting than the systematic release of the second MGF liver variant.

So just think of MGF as a highly anabolic variant of igf. After you have trained, the IGF-I gene is spliced towards MGF then that causes hypertrophy and repair of local muscle damage by activating the muscle stem cells as well as other important anabolic processes, including the above mentioned protein synthesis, and increased nitrogen retention.

In rats some studies have shown muscle mass increases of 20 percent from a single mgf injection.. somewhow i think many of these studies are not accurate, however the potential is undeniable.

Pegylated Mechano Growth Factor is a Research Peptide Hormone Mechano Growth Factor adds pegylation process to amino acid peptides synthesis is an original interlaced variant of IGF-1 (Insulin Like Growth Factor-I). MGF is a splice variant of the IGF gene which increases stem cell count in the muscle and allows for muscle fibers to fuse and mature. This is a process required for growth of adult muscle.

Mechano Growth Factor (MGF) also known as IGF-1Ec is a growth factor/repair factor that is derived from exercised or damaged muscle tissue, Its called MGF as IGF-1Ec is a bit of a mouthful and harder to identify amongst the other igf variants.
What makes MGF special is its unique role in muscle growth.
MGF has the ability to cause wasted tissue to grow and improve itself by activating muscle stem cells and increasing the upregulation of protein synthesis, this unique ability can rapidly improve recovery and speed up muscle growth.
MGF can initiate muscle satellite (stem) cell activation in addition to its IGF-Ireceptor domain which ithen in turn ncreases protein synthesis turnover, and therefore can if used correctly improve muscle mass over time.
The liver produces 2 kinds of MGF splice variants of igf..
1) IGF-1Ec This is the first phase release igf splice variant and it appears to stimulate satellite cells into activation, This is the closest variant to synthetic MGF.

2) liver type IGF-IEa this is the secondary release of igf from the liver, and its far less anabolic.

MGF differs from the second variant IGF-IEa as it has a different peptide sequence which is responsible for replenishing the satellite cells in skeletal muscle, in other words it is more anabolic and longer acting than the systematic release of the second MGF liver variant.

So just think of MGF as a highly anabolic variant of igf. After you have trained, the IGF-I gene is spliced towards MGF then that causes hypertrophy and repair of local muscle damage by activating the muscle stem cells as well as other important anabolic processes, including the above mentioned protein synthesis, and increased nitrogen retention.

In rats some studies have shown muscle mass increases of 20 percent from a single mgf injection.. somewhow i think many of these studies are not accurate, however the potential is undeniable.

The synthetic variant is known pharmaceutically as alprostadil.It is a drug used in the continuous treatment of erectile dysfunction. and has vasodilatory properties. Misoprostol is another synthetic prostaglandin E1 analog used to prevent gastric ulcers when taken on a continuous basis, to treat missed miscarriage, to induce labor, and to induce abortion.

Alprostadil is also used in maintaining a patent ductus arteriosus in newborns. This is primarily useful when the threat of premature closure of the ductus arteriosus exists in an infant with ductal-dependent congenital heart disease, including cyanotic lesions (e.g., pulmonary atresia/stenosis, tricuspid atresia/stenosis, transposition of the great arteries) and acyanotic lesions (e.g., coarctation of the aorta, hypoplastic left heart syndrome, critical aortic stenosis, and interrupted aortic arch).


Alprostadil is sold in the United States as urethral suppositories and in injectable form. The suppositories are sold under the brand name Muse. The injectable forms are Edex and Caverject. Muse delivers alprostadil as a penile suppository, inserted into the urethra, at least ten minutes before the erection is needed. Caverject and Edex are similarly fast-acting, but instead are injected by syringe directly into the corpus cavernosum of the penis.

Alprostadil is also available as a generic. The major cost is that it must be mixed by a compounding pharmacy and supplies may be difficult to obtain. The different formulations, including Bimix and Trimix, may include papaverine and/or phentolamine. A typical mix might be 30 mg of papaverine, 2 mg of phentolamine, and 20 μg alprostadil. As a generic, it is much less expensive than the packaged injectables. It is premixed and must be kept refrigerated and the user must load a syringe with the quantity needed.


Alprostadil is also used for critical limb ischemia. It increases blood flow by peripheral vasodilation within five minutes and induces angiogenesis. It is most effective when the ankle pressure is at least 30 mmHg and at least one tibial artery is patent.

Bremelanotide (formerly PT-141) is a compound under drug development by Palatin Technologies as a treatment for female sexual dysfunctionhemorrhagic shock and reperfusion injury. It functions by activating themelanocortin receptors MC1R and MC4R, to modulate inflammation and limiting ischemia. It was originally tested for intranasal administration in treating female sexual dysfunction but this application was temporarily discontinued in 2008 after concerns were raised over adverse side effects of increased blood pressure. As of March 2012, Palatin is conducting a human Phase 2B study using a new subcutaneous drug delivery system that appears to have little effect on blood pressure.

Bremelanotide was developed from the peptide hormone Melanotan II which underwent testing as a sunless tanningagent. In initial testing, Melanotan II did induce tanning but additionally caused sexual arousal and spontaneous erections as unexpected side effects in nine out of the ten original male volunteer test subjects.

Palatin completed patient treatment in its Phase 2B clinical trial in premenopausal women with FSD Primary data analysis and announcement of top-line results anticipated in first-half of fourth quarter of calendar year 2012 

In studies, bremelanotide was shown to induce lordosis in an animal model and was also effective in treating sexual dysfunction in both men (erectile dysfunction or impotence) and women (sexual arousal disorder). Unlike Viagra and other related medications, it does not act upon the vascular system, but directly increases sexual desire via the nervous system.

Phase III clinical trial was scheduled to begin in the first half of 2007, but was delayed until August 2007. On August 30, Palatin announced that the U.S. Food and Drug Administration had expressed serious concerns regarding therisk/benefit ratio of bremelanotide with regards to the side effect of increased blood pressure. The FDA stated that it would consider alternate uses for bremelanotide, including as a treatment for individuals who do not respond to more established ED treatments. However, On May 13, 2008, Palatin Technologies announced it had “discontinued development of Bremelanotide for the treatment of male and female sexual dysfunction” while concurrently announcing plans to develop it as a treatment for hemorrhagic shock instead. The company additionally announced intentions to focus its attention on another compound, PL-6983, that causes lower blood pressure in animal models. Palatin has since re-initiated Bremelanotide studies for ED and FSD using a subcutaneous delivery method. On August 12, 2009, the company announced that in a double-blind study of 54 volunteers bremelanotide failed to evoke the hypertensive side effects seen with the nasal delivery system used in prior studies, concluding that “variability of uptake” inherent in intranasal administration of the drug resulted in “increases in blood pressure and gastrointestinal events…primarily related to high plasma levels in [only] a subset of patients” and that subcutaneous administration of the drug circumvented the potential for this side effect. Palatin has completed a human Phase 2B study utilizing subcutaneous administration and reported positive results. 

Sermorelin (trade name is Geref) is a growth hormone releasing hormone (GHRH) analogue. It is a 29-amino acid polypeptiderepresenting the 1–29 fragment from endogenous human growth hormone releasing hormone, and is thought to be the shortest fully functional fragment of GHRH. It is used as a test for growth hormone secretion. It is also used as doping substance in sports

Sermorelin is an analog of the 1-29 fragment of the naturally occurring growth hormone releasing hormone (GHRH). This polypeptide is thought to be the shortest fully functioning fragment of growth hormone releasing hormone and contains the first 29 amino acids of GH. These are the active amino acids of GHRH that stimulate production in the pituitary gland



The thyroid hormones, triiodothyronine (T3) and its prohormone, thyroxine (T4), are tyrosine-based hormones produced by the thyroid gland that are primarily responsible for regulation of metabolism. Iodine is necessary for the production of T3 and T4. A deficiency of iodine leads to decreased production of T3 and T4, enlarges the thyroid tissue and will cause the disease known as simple goitre. The major form of thyroid hormone in the blood is thyroxine (T4), which has a longer half-life than T3.[1] The ratio of T4 to T3 released into the blood is roughly 20 to 1. T4 is converted to the active T3 (three to four times more potent than T4) within cells by deiodinases (5′-iodinase). These are further processed by decarboxylation and deiodination to produce iodothyronamine (T1a) and thyronamine (T0a). All three isoforms of the deiodinases are selenium-containing enzymes, thus dietary selenium is essential for T3 production. 

Contents  [hide]

1 Function

2 Production

2.1 Central

2.2 Peripheral

2.3 Initiation of production in fetuses

3 Effect of iodine deficiency on thyroid hormone synthesis

4 Circulation and transport

4.1 Plasma transport

4.2 Membrane transport

4.3 Intracellular transport

5 Measurement

6 Effects of thyroxine

7 Medical use

7.1 Formulations

8 Related diseases

9 Anti-thyroid drugs

10 See also

11 References

12 External links


The thyroid system of the thyroid hormones T3 and T4.[2]

The thyronines act on nearly every cell in the body. They act to increase the basal metabolic rate, affect protein synthesis, help regulate long bone growth (synergy with growth hormone) and neural maturation, and increase the body’s sensitivity to catecholamines (such as adrenaline) by permissiveness. The thyroid hormones are essential to proper development and differentiation of all cells of the human body. These hormones also regulate protein, fat, and carbohydrate metabolism, affecting how human cells use energetic compounds. They also stimulate vitamin metabolism. Numerous physiological and pathological stimuli influence thyroid hormone synthesis.

Thyroid hormone leads to heat generation in humans. However, the thyronamines function via some unknown mechanism to inhibit neuronal activity; this plays an important role in the hibernation cycles of mammals and the moulting behaviour of birds. One effect of administering the thyronamines is a severe drop in body temperature.

 Synthesis of the thyroid hormones, as seen on an individual thyroid follicular cell:[3]

– Thyroglobulin is synthesized in the rough endoplasmic reticulum and follows the secretory pathway to enter the colloid in the lumen of the thyroid follicle by exocytosis.

– Meanwhile, a sodium-iodide (Na/I) symporter pumps iodide (I-) actively into the cell, which previously has crossed the endothelium by largely unknown mechanisms.

– This iodide enters the follicular lumen from the cytoplasm by the transporter pendrin, in a purportedly passive manner.[4]

– In the colloid, iodide (I-) is oxidized to iodine (I0) by an enzyme called thyroid peroxidase.

– Iodine (I0) is very reactive and iodinates the thyroglobulin at tyrosyl residues in its protein chain (in total containing approximately 120 tyrosyl residues).

– In conjugation, adjacent tyrosyl residues are paired together.

– Thyroglobulin binds the megalin receptor for endocytosis back into the follicular cell.

– Proteolysis by various proteases liberates thyroxine and triiodothyronine molecules, which enter the blood by largely unknown mechanisms.

Iodothyronine deiodinase.png

Thyroid hormones (T4 and T3) are produced by the follicular cells of the thyroid gland and are regulated by TSH made by the thyrotropes of the anterior pituitary gland. The effects of T4 in vivo are mediated via T3 (T4 is converted to T3 in target tissues). T3 is 3- to 5- fold more active than T4.

Thyroxine (3,5,3′,5′-tetraiodothyronine) is produced by follicular cells of the thyroid gland. It is produced as the precursor thyroglobulin (this is not the same as TBG), which is cleaved by enzymes to produce active T4.

The steps in this process are as follows:

The Na+/I- symporter transports two sodium ions across the basement membrane of the follicular cells along with an iodide ion. This is a secondary active transporter that utilises the concentration gradient of Na+ to move I- against its concentration gradient.

I- is moved across the apical membrane into the colloid of the follicle.

Thyroperoxidase oxidises two I- to form I2. Iodide is non-reactive, and only the more reactive iodine is required for the next step.

The thyroperoxidase iodinates the tyrosyl residues of the thyroglobulin within the colloid. The thyroglobulin was synthesised in the ER of the follicular cell and secreted into the colloid.

Iodinated Thyroglobulin binds megalin for endocytosis back into cell.

Thyroid-stimulating hormone (TSH) released from the pituitary gland binds the TSH receptor ( a Gs protein-coupled receptor) on the basolateral membrane of the cell and stimulates the endocytosis of the colloid.

The endocytosed vesicles fuse with the lysosomes of the follicular cell. The lysosomal enzymes cleave the T4 from the iodinated thyroglobulin.

These vesicles are then exocytosed, releasing the thyroid hormones.

Thyroxine is produced by attaching iodine atoms to the ring structures of tyrosine molecules. Thyroxine (T4) contains four iodine atoms. Triiodothyronine (T3) is identical to T4, but it has one less iodine atom per molecule.

Iodide is actively absorbed from the bloodstream by a process called iodide trapping. In this process, sodium is cotransported with iodide from the basolateral side of the membrane into the cell and then concentrated in the thyroid follicles to about thirty times its concentration in the blood. Via a reaction with the enzyme thyroperoxidase, iodine is bound to tyrosine residues in the thyroglobulin molecules, forming monoiodotyrosine (MIT) and diiodotyrosine (DIT). Linking two moieties of DIT produces thyroxine. Combining one particle of MIT and one particle of DIT produces triiodothyronine.

DIT + MIT → r-T3 (biologically inactive)

MIT + DIT → triiodothyronine (usually referred to as T3)

DIT + DIT → thyroxine (referred to as T4)

Proteases digest iodinated thyroglobulin, releasing the hormones T4 and T3, the biologically active agents central to metabolic regulation.


Thyroxine is believed to be a prohormone and a reservoir for the most active and main thyroid hormone T3. T4 is converted as required in the tissues by iodothyronine deiodinase. Deficiency of deiodinase can mimic an iodine deficiency. T3 is more active than T4 and is the final form of the hormone, though it is present in less quantity than T4.

Initiation of production in fetuses[edit]

Thyrotropin-releasing hormone (TRH) is released from hypothalamus by 6 – 8 weeks, and thyroid-stimulating hormone (TSH) secretion from fetal pitutary is evident by 12 weeks of gestation, and fetal production of thyroxine (T4) reaches a clinically significant level at 18–20 weeks.[5] Fetal triiodothyronine (T3) remains low (less than 15 ng/dL) until 30 weeks of gestation, and increases to 50 ng/dL at term.[5] Fetal self-sufficiency of thyroid hormones protects the fetus against e.g. brain development abnormalities caused by maternal hypothyroidism.[6]

Beta thymosins are a family of proteins which have in common a sequence of about 40 amino acids similar to the small protein thymosin.  They are found almost exclusively in multicellular animals. Thymosin β4 was originally obtained from the thymus in company with several other small proteins which although named collectively “thymosins” are now known to be structurally and genetically unrelated and present in many different animal tissues.

Monomeric β-thymosins, i.e. those of molecular weight similar to the peptides originally isolated from thymus by Goldstein, are found almost exclusively in cells of multicellular animals.Known exceptions are monomeric thymosins found in a few single-celled organisms, significantly those currently regarded as the closest relatives of multicellular animals: choanoflagellates and filastereans. Although found in very early-diverged animals such as sponges, monomeric thymosins are absent from arthropods and nematodes, which do nevertheless possess “β-thymosin repeat proteins” which are constructed from several end-to-end repeats of β-thymosin sequences.Genomics has shown that tetrapods (land vertebrates) each express three monomeric β-thymosins, which are the animal species’ equivalents (orthologues) of human β4, β10 and β15 thymosins, respectively. The human thymosins are encoded by the genes TMSB4XTMSB10 and TMSB15A and TMSB15B. (In humans, the proteins encoded by the two TMSB15 genes are identical.) Bony fish in general express orthologues of these same three, plus an additional copy of the β4 orthologue.

The N-terminal half of β-thymosins bears a strong similarity in amino acid sequence to a very widely distributed sequence module, the WH2 module. (Wasp Homology Domain 2 – the name is derived from Wiskott-Aldrich syndrome protein).[10][11] Evidence from X-ray crystallography shows that this part of β-thymosins binds to actin in a near-identical manner to that of WH2 modules, both adopting as they bind, a conformation which has been referred to as the β-thymosin/WH2 fold. β-thymosins may therefore have evolved by addition of novel C-terminal sequence to an ancestral WH2 module. However, sequence similarity searches designed to identify present-day WH2 domains fail to recognise β-thymosins, (and vice versa) and the sequence and functional similarities may result from convergent evolution

Tesamorelin (trade name Egrifta) is a synthetic form of growth-hormone-releasing hormone (GHRH) which is used in the treatment ofHIV-associated lipodystrophy. Tesamorelin is produced and developed by Theratechnologies, Inc. of Canada.

Tesamorelin is a synthetic peptide consisting of all 44 amino acids of human GHRH with the addition of a trans-3-hexenoic acid group

Tesamorelin 10mg is a research compound developed in Canada by Theratechnologies. It belongs to synthetic hormones also called growth-hormone-releasing. These hormones are peptides and Tesamorelin, as one of them, consist of 44 amino acids.

Thymosin α1 is believed to be a major component of Thymosin Fraction 5 responsible for the activity of that preparation in restoring immune function in animals lacking thymus glands. It was the first of the peptides from Thymosin Fraction 5 to be completely sequenced and synthesized. Unlike β thymosins, to which it is genetically and chemically unrelated, thymosin α1is produced as a 28-amino acid fragment, from a longer, 113-amino acid precursor, prothymosin α.[3] It has been found to enhance cell-mediated immunity in humans as well as experimental animals.

Thymosin α1 is now approved in 35 under developed or developing countries for the treatment of Hepatitis B and C, and it is also used to boost the immune response in the treatment of other diseases


IGF-1 LR3, otherwise known as “Long R3 IGF-1” or “Insulin-Like Growth Factor-1 Long Arg3”. It’s a synthetic hormone from a family of proteins that boost hormone growth and that has most of the same properties as IGF-1 (insulin-like growth factor) – which occurs naturally in our bodies.

IGF-1 in the body is responsible for transporting amino acids to cells, increasing protein synthesis and increasing synthesis of RNA, decreasing degradation of protein, and increasing the transport of glucose. IGF-1 regulates the division of cells in the body which has led to the push for creating synthetic analogues of the molecule. It is hoped that the analogues will one day have the potential to fight cancer, decrease obesity, and improve or cure chronic muscle diseases and muscle wasting as a result of aging.

Scientists created the synthetic version of IGF-1, IGF-1 LR3, to increase growth hormone activity as it mimics the insulin structure. It is currently only available for research purposes. This protein is generally created as a response to growth hormones and plays a role in the formation and separating of new muscle cells – referred to as hyperplasia.


The pituitary gland secretes growth hormone. In clinical studies, IGF-1 LR3 helps assist with retaining muscle through splitting and forming new muscle cells (hyperplasia). It works by preventing insulin from transporting glucose across cell membranes. It’s the creation of new muscle while repairing older and damaged muscles. Studies show that muscle growth and muscle repair contributes to fat loss, improved physical performance, faster recovery after exercise or injury, and decreased aging results.

IGF-1 LR3 is made up of eighty-three amino acids.


Amino acids are basically the “building blocks” of proteins. The human body is made up of 20% of protein. Amino acids are also important in the body for transporting and storing nutrients, playing a role in the healing of wounds and tissues or removing waste deposits the body produces in connection with metabolism.


Rats are often used in studies involving research chemicals and peptides. In a study of rats with IGF-1 LR3, it was found that injecting the peptide into rats prevented muscle atrophy related to age, the process in which muscle fiber and connective tissue deteriorates as a result of the decrease in growth hormone and insulin. The 27 month old rats would have the same strength and speed as they did at 6 months old.


Researchers have used IGF-1 and its analogues in studies for Lou Gehrig’s Disease, Duchene Muscular Dystrophy, ALS, autism, and ALS. The studies generally compare the effects of giving IGF-1 or the derivatives in place of corticosteorids. In DMD, males receiving IGF-1 showed better growth and fewer neurological and cardiovascular side effects than corticosteorids. IGF-1 had little benefit for ALS since ALS is motorneuron related rather than muscle-wasting related, and results from studies involving IGF-1 and Rett syndrome and autism are not yet available.

More research involving the potential of IGF-1 LR3 for improving muscle wasting and as an anti-cancer agent is sure to take place. Maybe one day this synthetic hormone will be used as a medicine.


Home chemists and professional researchers love to experiment with research peptides whether in makeshift, home labs, or professional clinical laboratories. There are many peptides in currently being studied for their medicinal properties. If you’re going to conduct any type of research it’s important that you are buying research peptides from a reputable company so you know they are of high quality. Research chemicals should be handled by professional researchers.


Research peptides are available online from a variety of suppliers. Unfortunately, not all peptide suppliers are offering the quality and purity chemicals you need for accurate research results. When it comes to buying research peptides, you want to make sure you are choosing a reputable company so your research is valid.

But how do you know if you’re buying from a reputable company? Here’s what you should look for when evaluating different peptide suppliers:


To get reliable results from peptides you must ensure the chemicals are pure. A reputable peptide supplier will test every batch of peptides they receive before packaging and filling customer orders to make sure their customers receive the quality grade of peptides expected and paid for. Many suppliers will list their testing and purity results right on their website – but if you don’t see it, simply ask for the purity results of the lab testing before you me a purchase. A reputable company will gladly provide the results.


It’s pretty easy to spot a non-reputable peptide supplier. If you come across a website that is selling peptides and will sell them to athletes and bodybuilders for non-research purposes, you can be sure that is not a reputable peptide supplier. Make sure the website you’re considering buying peptides from indicates they are only selling peptides and research chemicals for research- not for human consumption.


In the US, research peptides must be of a minimum purity and meet safety standards that are higher than most any other country. When looking for a reputable company to buy your research peptides, it’s a good idea to look for peptides made and sold from the United States.


 Another sign of a reputable peptide supplier is that they know how to maintain the purity and quality of their research chemicals by storing them properly. Many peptides need to be stored in a freezer. Before making a peptide purchase, find out how the company intends to ship the peptides to you. Will they be frozen during the transport? Will they arrive at room temperature? Consider how the transport of chemicals might affect the accuracy of your research results.


If you want to learn more about a company’s reputation, check social media and websites for customer testimonials and reviews.  You can get a solid understanding of how a company deals with their customers and the quality of their products from what previous customers say about their purchases and experiences with the company. 


If after you’ve looked into all of the above when evaluating reputable companies for buying research peptides you’re still not sure – pick up the phone and call the suppliers customer service or send an email with any questions you have. They should answer you in a timely manner and be willing to answer any questions or address any concerns that you may have to help you decide whether or not you can buy the peptides from them.


PGE1 is an interesting therapy that has several uses for medications and therapies. Uses for PGE1 range from treating congenital heart defects to treating erectile dysfunction. PGE1 is a naturally occurring prostaglandin that was approved for medical use more than 35 years ago. What is PGE1 and why are so many researchers and medical professionals studying it?


As stated above, PGE1, also known as alprostadil is a prostaglandin. A prostaglandin is group hormones that the body creates when there is an injury or infection. Prostaglandins are the messengers and architects of healing injuries. Prostaglandins create inflammation and pain when an injury occurs, they kickstart blood clotting and controlling blood vessel walls, and well as dissipating blood clots to allow the walls of blood vessels to relax.

Medical and research uses for PGE1 is desired for its effects on smooth muscle. Smooth muscle is one of three types of muscle in the body: smooth, cardiac, and skeletal. Cardiac muscle is striated and under involuntary control. Cardiac muscle is the muscle in the heart. Skeletal muscle is what you think of when you lift weights or move your limbs. It is muscle attached to the bones. Skeletal muscle is striated and under voluntary control. Smooth muscle, the one PGE1 targets, is muscle that is under involuntary control. It is the muscle found inside the walls of visceral organs. 

Visceral organs with smooth muscle are found in GI systems, cardiovascular, respiratory and genitourinary systems. Genitourinary systems include the urinary and genital organs. Smooth muscle enables constriction and dilation to move fluids throughout the body. 

PGE1 is studied as an injectable, pellet or oral treatment, and powder.


Several clinical studies have been conducted with PGE1 (alprostadil). A 2008 systematic review of Prostaglandin E1 found that PGE1 pellets orally consumed or injected in the end of the penis treat erectile dysfunction and improve sexual satisfaction.

Studies have been conducted to evaluate the effectiveness prostaglandins to reduce ischaemic injury after organ transplants (2011), kidney disease (2010), and congenital heart defects at birth. Ischaemic injury can be classified based on its severity as either mild, moderate, or severe. Ischemic injury is the result of restricted blood supply to tissues. Dysfunction, defects, or other problems with the blood vessels cause ischemia. If a tissue cannot get get a healthy blood supply, it lacks oxygen to stay alive. As a result, the tissue dies.

2005 analysis of PGE1 also looked at the effectiveness of prostaglandins such as PGE1 for treating claudication. Claudication is pain or cramping in the lower limbs, and sometimes in the arms, during physical activity. The severe pain may be intermittent and it caused by inadequate blood flow to the area, usually caused by problems with the blood vessels. Symptoms of claudication include pain and discomfort in buttocks, legs, hips, calves, and feet. There may also be pain at rest or discoloration of lower limbs, digits, and arms. The 2005 study found that PGE1 is most effective and tolerated therapy for relieving pain and discomfort when moving.


Ostarine is a SARM that also goes by the name MK-2866. Ostarine was first developed by GTx. GTx is a company that has been studying the effects and benefits of SARMs, or selective androgen receptor modulators. SARMs bind to androgen receptor, but that are safer than steroid hormones. GTx did a study on Ostarine (enbosarm) studies with patients who have non-cell lung cancer. SARMs like Ostarine (MK-2866) are used in research to study the benefits to build muscle in those who suffer from muscle wasting diseases caused by illnesses.


Ostarine is a therapeutic compound that has the unique ability to create selective anabolic activity at specific androgen receptors. Anabolic is the action of synthesizing molecules in metabolism. Anabolism improves building muscle and performance. Androgen receptor (AR) plays an role in important reproductive and sex hormones, specifically regulating functions such as hormone production.  

SARMs target only the AR, as opposed to anabolic steroids that affect organs and entire systems. So, SARMs such as Ostarine MK-2866, when used for research purposes to treat muscle wasting, SARMs are safer for the body because they don’t produce dangerous side effects commonly associated with anabolic steroids.

Ostarine (MK-2866) is one of the most anabolic member of the SARMs family. This property alone is what makes it a highly desired compound in the research lab and clinics to promote lean muscle gain. Unlike anabolic steroids, it provides users with only lean muscle gain instead of bulk, bloat, and bad reactions. It can also run longer in the body when taken orally because it is non-methylated. 

MK-2866 does not have high toxicity levels, which means it won’t damage the liver when taken over longer periods of time and it won’t affect the blood pressure.


Research shows the Ostarine MK-2866 is a SARM that builds lean muscle and improves muscle performance in cancer patients who suffer from cancer cachexia, according to studies conducted by Merck and presented at the annual meeting of the Endocrine Society. 

Cancer cachexia is a condition that affects almost half of cancer patients in America. As they undergo cancer treatment, patients may experience significant weakness, immobility,  fatigue, and the loss of critical protein stores to maintain muscle and to have the strength to tolerate the life-saving cancer treatments. There are currently approved by the FDA for muscle wasting diseases caused by cancer, but research on products such as Ostarine MK-2866 show promise for those battling reduced muscle performance and production. 

As a whole, by improving anabolism of muscle tissue, Ostarine promotes bone function and health, curbing issues related to other ailments such as low bone density, injuries, and muscle motor dysfunction. When use for research purposes, adding Ostarine to a diet rich in lean proteins may improve its overall effectiveness. 

To recap, research has found that the oral compound Ostarine MK-2866 is an anabolic agent that improves lean mass gains, boosts strength, encourages healthy body recomposition, and may aid in joint, bone and muscle healing abilities not only in rodents in the lab but cancer patients and AIDs patients as well. 


Bacteriostatic water is a highly purified, sterilized water used to dissolve medications or dilute medications to the appropriate consistency for injection. Bacteriostatic water (BW) is a sterilized water that contains .9% benzyl alcohol and has a pH of about 5.7. The alcohol in the water helps prevent the growth of most forms of bacteria which makes it ideal for diluting any drug that will be administered by intramuscular, intravenous, or subcutaneous injection.

Bacteriostatic water is not used for neonatal medications because it contains benzyl alcohol, which is toxic, and can cause blood pressure changes in babies under four weeks of age. BW for injection is provided in unpressurized, 30 mL plastic vials, specially formulated from polyolefin. It is a copolymer of propylene and ethylene, and is considered safe plastic according to USP biological standards for plastic containers and the animal testing which took place to confirm its safety. The plastic container for bacteriostatic water doesn’t require a vapor barrier to maintain the proper volume. 

Most sources recommend that bacteriostatic water is used within 28 days of opening the vial. The preservatives will allow it to keep safely for up to 30 days.  


There are not many side effects associated with using bacteriostatic water. When there are side effects, it’s probably more related to the drug that is dissolved in the bacteriostatic water, or some sort of contamination of the water prior to use. 

If bacteriostatic water is injected by intravenous without a compound diluted in the water, it can cause red blood cell lysis. Lysis is the breaking down of a cell or membrane, which can be caused also by viruses or osmotic mechanisms which compromise the red blood cell’s integrity.

Side effects from bacteriostatic water have been reported to include:

  • Abscess formation
  • Death of tissues
  • Fever
  • Venous thrombosis or phlebitis
  • Infection at the site of injection
  • Febrile response

If using bacteriostatic water and you experience adverse side effects, discontinue use and check with a doctor. Save the unused water in case the doctor wants to inspect it for contamination or possible causes of adverse reactions.


While both bacteriostatic and sterilized water are sterile liquids, they do have some differences you should be aware of. You cannot simply replace bacteriostatic water with sterile water as they are not the same thing. 

Sterile water doesn’t have any preservatives in it to prolong its life, which means it can only be used for a single injection. It doesn’t have a shelf life once the container is opened and it has been used. Think of sterile water as single-use packages. 

 Bacteriostatic water contains benzyl alcohol as a preservative that prevents the growth of bacteria and allows the water to be used for multiple injections spread out over about 28 to 30 days. If your medication says to dilute or mix with bacteriostatic water, you do not want to substitute sterile water in its place or you risk getting an infection and experiencing adverse side effects.


Myostatin, also known as GDF-8 (Growth Differentiation Factor 8) is a myokine, which is a protein that is produced and released by myocytes that inhibits muscle cell growth and differentiation. Much research has been conducted on this natural protein found within humans and other animals because of the significant impact it can have on growth and development on muscle tissue and overall strength.

With that said, the research has been solely focused on animals that are either lacking in myostatin or treated with substances that block the activity of myostatin. The results of such research has presented findings of animals with significantly more muscle mass as a result of such treatments. The reason these studies are important is because of the potential therapeutic applications. Muscle wasting diseases such as muscular dystrophy could finally be treated if research in the laboratory could prove such medicinal use that is without negative or damaging side effects.


As mentioned, continued research of myostatin may potentially lead to a variety of therapies and uses for treating muscular dystrohphy and other muscle wasting diseases. Research conducted on mice and monkeys has proven that blocking or inhibiting myostatin does lead to an increase in muscle mass in both species. Additionally, there was a two-week study conducted on normal mice that led to a muscle mass increase of up to 60% by utilizing activin type IIB receptor – a molecule that attaches itself to cells and binds to myostatin.

Though, long-term treatment of muscle wasting diseases with myostatin inhibitors is unknown, at this time, to have beneficial effects research in the laboratory using animal test subjects continues.


A 2010 study was conducted by the Medical College of Georgia tested the hypothesis that a new myostatin inhibitor, a recombinant myostatin propeptide, would be able to enhance the repair and regeneration of muscle and bone in certain cases of severe injury. Test subjects for this particular study were lab mice. 

Mice were provided with the same injury types to their leg muscles and received injections once on the day of the surgery, one more injection five days after surgery, and a final injection 10 days after the surgery. Researchers utilized a micro-CT to determine the effectiveness of myostatin inhibitors in any potential enhancement of repair and regeneration of the injury sites after injections. The results of the research showed mice that received the myostatin injections experienced an increase in body mass of 7 percent and muscle mass increased by nearly 20 percent.

Additional research conducted in 2015 by Berno Dankbar discovered that myostatin deficiency also leads to a notable decrease in inflammation in and around bone fracture injuries. These findings could ultimately impact how diseases such as osteoporosis, muscular dystrophy, and other muscle and bone wasting diseases could potentially be treated one day. However, much more research is required and myostatin inhibitors are still strictly for scientific research purposes only. The impact on the human body upon consumption is unknown and considered dangerous.


Epitalon, also known as Epithalon or Epithalone, is a synthetic version of Epithalamin, a polypetptide, which humans produce naturally. The natural version of Epitalon, Epithalamin, was first discovered by Professor Vladimir Khavinson in Russia in the 1980s and has been studied extensively in the lab ever since its discovery. It is currently in continues clinical studies in Russia. Prospective results of preliminary studies show Epitalon has potential uses for geriatrics, liver disorders, neuropathy, mental health, and the slowing of cellular aging. 

This peptide is made up of four amino acids, which are alanine, aspartic acid, glutamic acid, and glycine. There have been many scientific studies of the benefits of Epitalon and it is currently available for research purposes only.


The primary purpose of Epitalon is to increase the natural production of telomerase, which is a natural enzyme that helps protect DNA. What this does is allow for the replication of DNA so new cells can be grown to rejuvenate old or damaged ones. FDA approved studies in controlled scientific experiments concerning telomerase have shown that longer telomere strands directly correlate to better overall cell health. Additionally, a telemerase study conducted on 913 pairs of twins showed that the twin with stronger telemerase production was in far better healthy and looked much younger than his/her twin counterpart.

Scientists continue to conduct extensive research on animal subjects with Epitalon because it has shown to increase the production of telomerase. The telomerase, of course, in turn helps to strengthen and lengthen telomeres and has proven anti-aging capabilities.

Research breakthroughs over the previous 35 years have proven that Epitalon is the only known peptide or substance that has shown an ability to increase telemerase production and strand length in animal subjects.


During scientific experiments in a controlled laboratory environment, animal cells and organs exposed to Epitalon are showing is an elongation of telomere – which is partly responsible for the aging of cells. Results of such studies in the laboratory on animal cells and organs have been such that that aging process in those cells and organs have either slowed down, stopped temporarily, or begun to reverse the effects of aging at the cellular level. What this boils down to is Epitalon has shown promise, in controlled research environments using animal test subjects, to increase the average lifespan in animal test subjects such as rats, mice, and fruit flies.

In a study on fruit flies, when Epitalon was administered during the larval stage results showed an increase in lifespan by upwards of 16 percent.

study on rats, who were exposed to identical amounts of light and darkness, fluctuating amounts of light and darkness, and permanent light illumination, the peptide was able to increase maximal lifespan in all three controlled groups by 68 days, 95 days, and 24 days.

Finally, a study of hypertension in mice showed an increase in maximal lifespan by 12.3 percent.


As of this writing, there have been no documented harmful side effects of Epitalon in clinical trials and scientific research on animal subjects. 

While Epitalon has shown much promise in the way of studying the effects of aging and how to reverse or slow it when using animal test subjects, Epitalon is not recommended for human consumption. It is presumed that human ingestion of Epitalon is dangerous and would have long-term, harmful effects on the human body. As with any research peptide, researchers should follow proper procedures when handling Epitalon and should not use it for anything other than legitimate research purposes.