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Product Attributes CAS # : 170851-70-4 Molecular Formula : C38H49N9O5 Sequence (AA) : Aib-His-D-2-Nal-D-Phe-Lys-NH2 Molecular Weight : 711.86 g/mol PubChem CID : 9831659 Half-Life : ~2 hours Synonyms : NNC 26-0161, Ipamorelin acetate Type : Synthetic research peptide (selective growth hormone secretagogue, GHRP) Research Focus : Growth Hormone Modulation, Recovery & Performance, Longevity & Anti-Aging Scientific References Ipamorelin, the first selective growth hormone secretagogue Animal | In vitro Growth hormone secretagogues: history, mechanism of action and clinical development Observational | Animal | In vitro The growth hormone-releasing effect of ipamorelin in human volunteers Human RCT | Observational Ipamorelin prevents bone loss and accelerates fracture healing in ovariectomized rats Animal Ghrelin receptor signaling: a promising therapeutic target Animal | In vitro Effects of ipamorelin on body composition and bone formation in growing rats Animal Ulimorelin and ipamorelin in postoperative ileus: phase 2 clinical trial Human RCT Ipamorelin: research summary on growth hormone release and tolerability Observational | Animal Included In The Box Every product arrives in a premium, custom-designed PEPTIDE.Power box , engineered for convenience, hygiene, and safe storage in your refrigerator
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[2] Contents: Molecular Characterization and Essential Functions Copper Peptides Scientific Research and Studies BPC157 and Tendon Fibroblast Signaling: PAK-Paxillin Pathway Modulation Growth Hormone Receptor Upregulation in Fibroblast Populations BPC157 and VEGFR2-Mediated Angiogenic Signaling BPC157 in Gastrointestinal Mucosal and Systemic Cytoprotection Models Musculoskeletal Tissue Repair: Narrative Review Data (2025) BPC157 and Neurotransmitter System Modulation: Brain-Gut Axis Research BPC157 as a Putative Neurotransmitter-Like Cytoprotective Mediator Central Nervous System Repair: Neuroregeneration Research References Molecular Characterization and Essential Functions BPC157 is distinguished among synthetic research peptides by its resistance to enzymatic degradation in gastric environments, a property attributed to its partial origin from an endogenous gastric protein sequence
