MSDS
3RD PARTY TEST RESULT
GHRP-6
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
Tax included
Molecular Formula:
C46H56N12O6
Molecular Weight:
873
Monoisotopic Mass:
872.44457755
Polar Area:
301
Complexity:
1570
XLogP:
1.9
Heavy Atom Count:
64
Hydrogen Bond Donor Count:
11
Hydrogen Bond Acceptor Count:
9
Rotatable Bond Count:
23
PubChem LCSS:
Growth hormone releasing hexapeptide 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
GHRP-6 is a synthetic growth hormone secretagogue peptide that serves as an agonist of the ghrelin/growth hormone secretagogue receptor (GHSR1a), a G protein–coupled receptor involved in neuroendocrine signaling. In research settings, GHRP-6 is used as a tool compound to investigate how ghrelin-pathway activation influences pituitary hormone release, appetite-related circuitry, and downstream intracellular signaling. Most research focuses on receptor pharmacology (including binding characteristics, potency, and desensitization), mapping of signaling pathways activated after GHSR1a engagement, and characterization of endocrine secretion patterns in controlled in vitro systems and preclinical models. Findings depend on experimental context, including the model organism, tissue type, dosing paradigm, and assay selection.
Biochemical Characteristics
GHRP-6 is a short, synthetic peptide containing both L- and D-amino acid residues. The presence of D-configuration residues is frequently leveraged in research peptides to modulate proteolytic susceptibility and receptor-interaction profiles in experimental settings. As a receptor tool compound, GHRP-6 is used to activate GHSR1a to quantify ligand–receptor interactions, compare agonist activity, and evaluate downstream pathway activation kinetics. In endocrine pharmacology research history, growth hormone-releasing peptides (GHRPs) were characterized as synthetic secretagogues that stimulate growth hormone release in experimental settings, supporting their adoption as tools for mapping receptor biology and neuroendocrine signaling circuits.[13]
Research Applications
GHRP-6 is studied in vitro and in animal models to evaluate GHSR1a-mediated signaling and physiological readouts that can be quantified under laboratory conditions. In cell-based assays, researchers commonly measure receptor activation using endpoints such as second-messenger readouts (assay-dependent), phosphorylation markers in downstream pathways, reporter gene activity, and receptor internalization/desensitization metrics. These outcomes are typically analyzed relative to vehicle-treated controls and may be further compared across concentration ranges to generate potency and efficacy profiles. In endocrine-focused models, investigators frequently quantify growth hormone release over time, including secretion kinetics and pulse characteristics, and compare results with baseline or matched control groups. In appetite and metabolism research, common endpoints include food intake, meal patterning, body weight trajectory, and metabolic marker panels, interpreted as changes observed relative to controls rather than as evidence of clinical effect. In neuroscience-oriented studies, researchers may examine region-specific signaling markers, gene expression changes, or behavioral task performance as endpoints, often incorporating antagonist conditions or receptor perturbation (e.g., knockdown/knockout) to support receptor-specific interpretation. The information presented in this article is provided solely for scientific, educational, and laboratory reference purposes. Any products or materials referenced are intended exclusively for in-vitro laboratory research use and are not intended for human or animal use, including diagnosis, treatment, mitigation, or prevention of any disease. No content herein should be construed as medical, clinical, or therapeutic guidance.
Pathway / Mechanistic Context
GHRP-6 is employed to activate the growth hormone secretagogue receptor (GHSR1a), a G protein-coupled receptor (GPCR) that participates in neuroendocrine signaling and metabolic sensing networks. In experimental systems, GHSR1a activation is used to characterize GPCR-driven signal transduction (including G protein- and kinase-associated cascades) and to quantify downstream changes in transcriptional programs relevant to cellular stress responses, inflammatory signaling, and apoptosis-related pathways. Historically, the identification of a dedicated growth hormone secretagogue receptor and the subsequent discovery of endogenous ligand biology helped establish a mechanistic framework for using synthetic agonists (including GHRPs) as experimental probes of ghrelin/GHSR signaling.[14], [15] Within the central nervous system, ghrelin/GHSR signaling is used experimentally to evaluate synaptic plasticity and circuit-level modulation in discrete regions (e.g., amygdala- and hippocampus-associated paradigms) and to map receptor expression patterns in anatomically defined nuclei implicated in motor control and dopaminergic signaling. In peripheral tissues, pathway-focused work has explored GHSR-linked modulation of oxidative stress readouts, cytokine-associated signaling, and extracellular matrix remodeling signatures.
Preclinical Research Summary
Neural plasticity and memory-related paradigms (rodent studies) Preclinical studies have used ghrelin pathway modulation to examine learning- and memory-associated endpoints and synaptic plasticity measures in rodents. In these experimental contexts, GHSR signaling has been implicated in the regulation of extinction learning, long-term depression in the amygdala, and memory encoding processes. Related work has evaluated spatial learning outcomes following localized ghrelin pathway manipulations in the amygdala in rodent models.[1], [2], [3] Ischemic brain injury models (preclinical) In animal models designed to study ischemia-associated injury cascades, ghrelin pathway agonism has been investigated for its effects on apoptosis-associated markers and neuroinflammatory signaling. These models are used to quantify molecular and histologic correlates of injury and to characterize timing-dependent pathway effects in preclinical settings.[4], [5] Dopaminergic system and substantia nigra receptor mapping (rodent studies) Preclinical research has reported ghrelin receptor expression in the substantia nigra and has explored how altered receptor expression relates to motor dysfunction phenotypes in genetic and pharmacologic rodent paradigms. These studies are commonly used to assess receptor expression changes, pathway responsiveness to agonism/antagonism, and apoptosis-associated endpoints in dopaminergic neuron populations under controlled experimental conditions.[6] Extracellular matrix remodeling and proteome-level profiling (animal wound models) In rat wound-model systems, GHRP-6 and related pathway probes have been used to investigate tissue remodeling dynamics, including extracellular matrix protein deposition patterns and proteome-level shifts during the remodeling phase. Reported endpoints include collagen-associated signatures, matrix organization measures, and broader protein expression changes observed in mechanistic surveys.[7], [8] Oxidative stress endpoints in myocardial injury models (large-animal studies) Porcine myocardial injury models have been used to evaluate whether ghrelin pathway agonism modulates oxidant-associated cytotoxicity readouts and necrosis-related markers. These studies typically quantify biochemical injury indices, histologic changes, and oxidative stress-associated endpoints to characterize pathway involvement in tissue stress responses in vivo.[9] Motivation and reward-seeking behavior paradigms (rodent studies) Rodent behavioral studies have examined how central ghrelin receptor stimulation modulates motivated behavior in a site-dependent manner. Experimental designs commonly use receptor agonists and antagonists to localize functional contributions of specific brain regions to reward-seeking and motivated behavioral outputs.[10]
Form & Analytical Testing
Material is supplied as a research reagent intended for laboratory experimentation. Product identity and analytical characterization are typically established using standard peptide quality control approaches (e.g., chromatographic purity assessment and mass-based identity confirmation) consistent with research reagent expectations. Researchers should select storage, handling, and reconstitution conditions appropriate to peptide materials and compatible with their specific experimental design, analytical platform, and institutional laboratory practices.
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
Márta Korbonits graduated in Medicine in Budapest and undertook her early clinical training at the Internal Medicine Department of the Postgraduate Medical School, Budapest. She joined the Department of Endocrinology at St. Bartholomew’s Hospital under the mentorship of Professors Ashley Grossman and Michael Besser. Her MD and later PhD studies contributed to the understanding of the effects of growth hormone secretagogues on hypothalamic hormone release and the nature and causes of pituitary tumorigenesis. She was awarded an MRC Clinician Scientist Fellowship and commenced studies that produced novel insights into ghrelin physiology and genetics. Her findings related to the regulation of the metabolic enzyme AMPK by ghrelin, cannabinoid and glucocorticoid opened a new aspect of hormonal regulation of metabolism. In 2008, Márta Korbonits was promoted to Professor of Endocrinology and Metabolism and since 2012, has led the Centre of Endocrinology at Barts and the London School of Medicine. In 2016, Márta Korbonits was appointed a Deputy Head of the William Harvey Research Institute. Professor Korbonits continues to integrate human studies alongside with laboratory-based research and has pioneered several projects in translational medicine. Márta Korbonits is referenced as a scientist with published contributions related to growth hormone secretagogues and ghrelin physiology. This reference does not imply endorsement or advocacy of purchase, sale, or use of this product. No affiliation or relationship, implied or otherwise, is stated between the seller and this scientist. The referenced work appears in the citations list below.
Referenced Citations
C.-C. Huang, D. Chou, C.-M. Yeh, and K.-S. Hsu, “Acute food deprivation enhances fear extinction but inhibits long-term depression in the lateral amygdala via ghrelin signaling,” Neuropharmacology, vol. 101, pp. 36–45, Feb. 2016. S. Beheshti and S. Shahrokhi, “Blocking the ghrelin receptor type 1a in the rat brain impairs memory encoding,” Neuropeptides, vol. 52, pp. 97–102, Aug. 2015. K. Tóth, K. László, and L. Lénárd, “Role of intraamygdaloid acylated-ghrelin in spatial learning,” Brain Res. Bull., vol. 81, no. 1, pp. 33–37, Jan. 2010. N. Subirós et al., “Assessment of dose-effect and therapeutic time window in preclinical studies of rhEGF and GHRP-6 coadministration for stroke therapy,” Neurol. Res., vol. 38, no. 3, pp. 187–195, Mar. 2016. S. J. Spencer, A. A. Miller, and Z. B. Andrews, “The Role of Ghrelin in Neuroprotection after Ischemic Brain Injury,” Brain Sci., vol. 3, no. 1, pp. 344–359, Mar. 2013. Y. Suda et al., “Down-regulation of ghrelin receptors on dopaminergic neurons in the substantia nigra contributes to Parkinson’s disease-like motor dysfunction,” Mol. Brain, vol. 11, no. 1, p. 6, 2018. Y. Mendoza Marí et al., “Growth Hormone-Releasing Peptide 6 Enhances the Healing Process and Improves the Esthetic Outcome of the Wounds,” Plastic Surgery International, 2016. M. Fernández-Mayola et al., “Growth hormone-releasing peptide 6 prevents cutaneous hypertrophic scarring: early mechanistic data from a proteome study,” Int. Wound J., vol. 15, no. 4, pp. 538–546, Aug. 2018. J. Berlanga et al., “Growth-hormone-releasing peptide 6 (GHRP6) prevents oxidant cytotoxicity and reduces myocardial necrosis in a model of acute myocardial infarction,” Clin. Sci. (Lond.), vol. 112, no. 4, pp. 241–250, Feb. 2007. L. Hyland et al., “Central ghrelin receptor stimulation modulates sex motivation in male rats in a site dependent manner,” Horm. Behav., vol. 97, pp. 56–66, 2018. H.-J. Huang et al., “The protective effects of Ghrelin/GHSR on hippocampal neurogenesis in CUMS mice,” Neuropharmacology, May 2019. Korbonits, Marta, and Ashley B. Grossman. “Growth Hormone-Releasing Peptide and Its Analogues.” Trends in Endocrinology & Metabolism, vol. 6, no. 2, Mar. 1995, pp. 43–49. Bowers CY et al., “(Growth hormone-releasing peptide research),” Endocrinology, 1990;126(3):1223–1228. Smith RG et al., “(Growth hormone secretagogue receptor / related discovery),” Science, 1997;275(5304):1261–1264. Kojima M et al., “Ghrelin discovery,” Nature, 1999;402(6762):656–660. 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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