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3RD PARTY TEST RESULT
GHRP-2 5mg
AOD-9604, lipolytic peptide fragment, which was derived from human growth hormone (HGH) during the late 1990s was modified from HGH residues 176-191. This modified compound primarily works as an element for fat burning and obesity treatment, while the exact mechanism by which this happens is still under research. It stimulates the breakdown (metabolism) of fat stores and inhibits the formation of fats without any detected side effects, affecting blood sugar levels or causing abnormal growth. In addition, the peptide shows several, apparently independent, positive effects on cartilage regeneration, improvement of metabolism or heart activity, confirmed by research.
€37.99
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Molecular Formula:
C45H55N9O6
Molecular Weight:
818
Monoisotopic Mass:
817.42753051
Polar Area:
256
Complexity:
1440
XLogP:
2.5
Heavy Atom Count:
60
Hydrogen Bond Donor Count:
9
Hydrogen Bond Acceptor Count:
8
Rotatable Bond Count:
21
PubChem LCSS:
Pralmorelin Laboratory Chemical Safety Summary
1 Usage of peptide
The product is intended for scientific research and development purposes only. Chemical substances shall not be used as a drug, medicine, active substance, medical aid, cosmetic product, a substance for production of a cosmetic product neither for human consumption that is any food or food supplement or otherwise similarly used on humans or animals. Intended only for in-vitro research, such as Receptor-ligand binding studies, Enzyme activity assays, Cell proliferation assays, Cell signaling assays, Epitope mapping, ect.
2 Peptides in transport
Peptides in lyophilized form are supplied in glass vials by standard shipping methods and do not require refrigeration. Short-term temperature fluctuations during transport will not reduce their quality and efficacy. Even at high summer temperatures, the peptides in lyophilized form are stable for several weeks.
3 Storage of lyophilized peptides
Upon receiving the lyophilized peptide, store at 4 °C or colder and away from bright light. Lyophilized peptides are stable at room temperature for weeks, but for longer-term storage, it is safer to store at -20 °C or colder. Exposure to moisture will greatly decrease long-term stability of lyophilized peptides. Before using the peptide, remove from cold storage and allow the peptide to equilibrate to room temperature before removing the lid of the container, in order to reduce the uptake of moisture that is present in the surrounding atmosphere.
4 Storage of peptide solutions
The shelf life of peptide solutions is limited. Freezing the aliquots will prolong the storage life of the peptide. What is globally accepted for peptides in solution is that they are generally stable for 3 or more weeks at +4°C and for 3-4 months at -20°C. Avoid repeated freeze-thaw cycles, as this can degrade the peptides.
Description of AOD-9604
A synthetically produced peptide AOD-9604 consists of 15 amino acids. It is derived fragment of human growth hormone (fragment 176-191) known mainly for its lipolytic qualities, thanks to which it can perfectly stimulate body fat burning without negative side effects, that are mainly perceived by using common weight loss drugs. Study has shown that it has a very good tolerability and safety, thus the immune system does not form any antibodies against the AOD-9604 peptide. Other great benefit seems to be that blood sugar levels are not affected. However, several studies have also shown that chronic treatment with AOD-9604 had no adverse effect on insulin sensitivity of researched animals. So, the peptide does not appear to affect IGF-1 or insulin levels at all.
Now we would like to bring you closer to the effects of the peptide, which have been researched and confirmed in studies.
[1] [2]
Research Confirmed Effects
Overview
Growth Hormone-Releasing Peptide-2 (GHRP-2, pralmorelin) is a synthetic hexapeptide widely utilized as a laboratory research compound for investigating growth hormone secretagogue receptor (GHSR1a) signaling and associated downstream molecular pathways. As one of the earliest characterized members of the growth hormone secretagogue class, GHRP-2 is commonly employed in receptor pharmacology, endocrine signaling studies, and mechanistic investigations of ghrelin-related pathways in controlled experimental systems. Within preclinical research settings, GHRP-2 functions as a selective agonist of GHSR1a and is used to interrogate receptor activation kinetics, signal transduction cascades, and tissue-specific receptor expression. All findings associated with GHRP-2 originate from in-vitro systems or in-vivo animal models and are interpreted strictly within a non-clinical, laboratory research framework.
Biochemical Characteristics
GHRP-2 is composed of six amino acid residues, including multiple D-amino acids that confer altered conformational stability and resistance to enzymatic degradation in experimental environments. The peptide structure supports high-affinity interaction with GHSR1a, making it a useful molecular probe for comparative ligand–receptor interaction studies and structure–activity relationship analyses. In biochemical assays, GHRP-2 is routinely applied to quantify receptor binding affinity, downstream second-messenger activation, and modulation of transcriptional outputs associated with ghrelin receptor signaling networks. Early endocrine research on growth hormone-releasing peptides (GHRPs) helped establish this peptide class as experimental secretagogues for probing neuroendocrine signaling.[12], [13]
Research Applications
GHRP-2 is employed in laboratory research to support mechanistic investigations across multiple biological domains, including: Receptor pharmacology: evaluation of GHSR1a activation, ligand specificity, and downstream signaling dynamics in cell-based assays. Muscle biology: analysis of protein synthesis and degradation pathways, including ubiquitin–proteasome system components, in animal and cellular models. Energy balance and feeding circuits: mapping ghrelin receptor involvement in hypothalamic and peripheral signaling networks regulating nutrient sensing in preclinical models. Cardiac cell stress models: investigation of apoptosis-associated markers and oxidative stress pathways in cardiomyocyte cultures and animal myocardial injury paradigms. Immunology research: examination of thymic signaling pathways and T-cell maturation processes influenced by ghrelin-associated endocrine signaling in animal studies. Neurobiology: exploration of sleep architecture regulation, nociceptive processing, and receptor crosstalk in rodent and murine models.
Pathway / Mechanistic Context
GHRP-2 activates the growth hormone secretagogue receptor (GHSR1a), a G protein-coupled receptor involved in neuroendocrine communication and metabolic sensing. Experimental activation of GHSR1a initiates intracellular signaling cascades that include G protein-mediated pathways, kinase activation, and modulation of gene expression relevant to cellular growth regulation, stress response, and metabolic coordination. Beyond classical endocrine signaling, GHSR1a activation by GHRP-2 has been used to investigate receptor distribution in peripheral tissues and the central nervous system. Preclinical findings indicate receptor-mediated modulation of pathways associated with muscle protein turnover, cardiomyocyte apoptosis, thymic cellular output, sleep-stage regulation, and supraspinal nociceptive processing. The identification of a dedicated growth hormone secretagogue receptor provided a central framework for using synthetic agonists (including GHRP-2) as tools to map ghrelin/GHSR signaling and GPCR pathway behavior in experimental models.[14]
Preclinical Research Summary
Muscle protein turnover models Animal studies, including large-animal and livestock models, have examined the effects of GHRP-2 on muscle protein deposition and degradation pathways. Reported outcomes include modulation of ubiquitin ligases such as atrogin-1 and MuRF1 and altered balance between anabolic and catabolic signaling in skeletal muscle tissue under growth-restricted conditions.[1], [2], [3] Feeding behavior and metabolic signaling Rodent and other preclinical models have demonstrated that ghrelin receptor agonism influences hypothalamic circuits involved in nutrient intake and energy balance. These models are used to quantify food intake patterns, endocrine signaling changes, and receptor-mediated behavioral outputs.[4], [5] Cardiomyocyte apoptosis studies Cell culture and animal-based myocardial stress models have utilized GHRP-2 and related peptides to evaluate apoptosis-associated signaling and oxidative stress markers. These investigations support ongoing efforts to characterize ghrelin receptor involvement in cardiac cellular stress responses.[6], [7] Thymic signaling and immune cell development Preclinical immunology research has explored how ghrelin-associated signaling pathways influence thymic architecture and T-cell maturation processes. These studies typically assess thymic output, cellular diversity, and signaling pathway engagement in aging or stress-related animal models.[8] Sleep architecture and neuroendocrine rhythms Experimental models examining sleep–wake regulation have used ghrelin receptor agonists to analyze changes in sleep-stage distribution and neuroendocrine rhythm modulation. Outcomes are assessed using electrophysiologic and behavioral endpoints in controlled laboratory settings.[9] Nociception and opioid receptor interaction Murine studies have reported that GHRP-2 interacts with supraspinal opioid receptor systems, enabling investigation of selective receptor engagement and pain-processing pathways. These models are used to study receptor specificity and signaling overlap between ghrelin and opioid systems.[10]
Form & Analytical Testing
This material is supplied as a laboratory research reagent. Identity and purity are typically verified using analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry (MS). Handling, storage, and experimental use should be conducted in accordance with institutional laboratory protocols and applicable regulatory requirements for research-only materials.
Article Author
The above literature was researched, edited and organized by Dr. Logan, M.D. Dr. Logan holds a doctorate degree from Case Western Reserve University School of Medicine and a B.S. in molecular biology.
Scientific Journal Author
Jean-Alain Fehrentz was born in Nancy, France, in 1955. He received his Ph.D. degree in Chemistry from the University of Nancy in 1983 and joined the Centre CNRS-INSERM de Pharmacologie Endocrinologie of Montpellier in the research group of Professor B. Castro. From 1989 to 1992 he was appointed as researcher at Sanofi Research in Montpellier. Then he moved to the Faculty of Pharmacy of Montpellier, working under the direction of Professor J. Martinez. His research interests focus on peptide aldehydes, enzyme inhibitors, peptidomimetics, growth hormone interactions, and heterocycle based receptor ligands. He has published more than 150 scientific papers. Jean-Alain Fehrentz is referenced here to acknowledge published work related to ghrelin receptor ligands and growth hormone secretagogues. This reference does not imply endorsement or advocacy of purchase, sale, or use of this product. No affiliation or relationship is implied between the seller and this scientist. A representative publication is included within the citations below.
Referenced Citations
R. Hu et al., “Effects of GHRP-2 and Cysteamine Administration on Growth Performance, Somatotropic Axis Hormone and Muscle Protein Deposition in Yaks (Bos grunniens) with Growth Retardation,” PloS One, vol. 11, no. 2, p. e0149461, 2016. D. Yamamoto et al., “GHRP-2, a GHS-R agonist, directly acts on myocytes to attenuate the dexamethasone-induced expressions of muscle-specific ubiquitin ligases, Atrogin-1 and MuRF1,” Life Sci., vol. 82, no. 9–10, pp. 460–466, Feb. 2008. L. T. Phung et al., “The effects of growth hormone-releasing peptide-2 (GHRP-2) on the release of growth hormone and growth performance in swine,” Domest. Anim. Endocrinol., vol. 18, no. 3, pp. 279–291, Apr. 2000. B. Laferrère, C. Abraham, C. D. Russell, and C. Y. Bowers, “Growth hormone releasing peptide-2 (GHRP-2), like ghrelin, increases food intake in healthy men,” J. Clin. Endocrinol. Metab., vol. 90, no. 2, pp. 611–614, Feb. 2005. B. Laferrère, A. B. Hart, and C. Y. Bowers, “Obese subjects respond to the stimulatory effect of the ghrelin agonist growth hormone-releasing peptide-2 on food intake,” Obesity (Silver Spring), vol. 14, no. 6, pp. 1056–1063, Jun. 2006. G. Muccioli et al., “Growth hormone-releasing peptides and the cardiovascular system,” Ann. Endocrinol., vol. 61, no. 1, pp. 27–31, Feb. 2000. V. Bodart et al., “Identification and characterization of a new growth hormone-releasing peptide receptor in the heart,” Circulation Research, vol. 85, no. 9, pp. 796–802, Oct. 1999. D. D. Taub, W. J. Murphy, and D. L. Longo, “Rejuvenation of the aging thymus: growth hormone-mediated and ghrelin-mediated signaling pathways,” Curr. Opin. Pharmacol., vol. 10, no. 4, pp. 408–424, Aug. 2010. G. Copinschi et al., “Prolonged oral treatment with MK-677, a novel growth hormone secretagogue, improves sleep quality in man,” Neuroendocrinology, vol. 66, no. 4, pp. 278–286, Oct. 1997. P. Zeng et al., “Ghrelin receptor agonist, GHRP-2, produces antinociceptive effects at the supraspinal level via the opioid receptor in mice,” Peptides, vol. 55, pp. 103–109, May 2014. A. Moulin, J. Ryan, J. Martinez, and J.-A. Fehrentz, “Recent Developments in Ghrelin Receptor Ligands,” ChemMedChem, vol. 2, pp. 1242–1259, 2007. Bowers CY et al., Endocrinology, 1990;126(3):1223–1228. Jacks T et al., Endocrinology, 1994;134(2):744–750. Smith RG et al., Science, 1997;275(5304):1261–1264. ALL ARTICLES AND PRODUCT INFORMATION PROVIDED ON THIS WEBSITE ARE FOR INFORMATIONAL AND EDUCATIONAL PURPOSES ONLY.
RUO Disclaimer
The products offered on this website are furnished for in-vitro studies only. In-vitro studies (Latin: in glass) are performed outside of the body. These products are not medicines or drugs and have not been approved by the FDA to prevent, treat or cure any medical condition, ailment or disease. Bodily introduction of any kind into humans or animals is strictly forbidden by law. For Laboratory Research Only. Not for human use, medical use, diagnostic use, or veterinary use.
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