Description

HGH Fragment 176–191

Synthetic C-terminal peptide fragment of human growth hormone (hGH 176–191 with an intramolecular disulfide bond Tyr176–Phe191) for in vitro research on selective lipolysis, lipogenesis inhibition, β3-adrenergic signaling, and adipocyte metabolism without mitogenic or glycemic alterations

Overview & Mechanism of Action (In Vitro)

HGH Fragment 176–191 (also designated as the lipolytic domain of hGH or an AOD-9604 analogue without the N-terminal tyrosine) is a synthetic 16-amino acid polypeptide derived from the C-terminal sequence of human growth hormone. It features an intramolecular disulfide bridge between two cysteine residues (Cys7-Cys14 within the peptide; equivalent to Cys182-Cys189 of full-length hGH), which stabilizes the bio-active loop essential for selective lipid mobilization. In molecular endocrinology, adipocyte biology, and metabolic physiology, it serves as the primary reference standard for isolating lipolytic pathways from general somatotropic signaling:

• Selective Induction of Adipocyte Lipolysis: Directly stimulates the hydrolysis of stored intracellular triglycerides into glycerol and free fatty acids by upregulating the expression and catalytic activity of hormone-sensitive lipase (HSL) in vitro.
• Inhibition of De Novo Lipogenesis: Suppresses fatty acid accumulation and lipid droplet formation by downregulating rate-limiting lipogenic enzymes, including fatty acid synthase (FAS) and acetyl-CoA carboxylase (ACC), in differentiated adipocyte cultures (such as 3T3-L1).
• β3-Adrenergic & cAMP Pathway Modulation: Activates adenylyl cyclase and drives intracellular cAMP accumulation via the specialized lipid-mobilizing domain without requiring full growth hormone receptor (GHR) engagement.
• Absence of Mitogenic & Diabetogenic Signatures: Lacks affinity for IGF-1 stimulating pathways and does not impair insulin-stimulated GLUT4 glucose transporter translocation, leaving basal glucose metabolism unaltered in vitro.

Technical & Chemical Specifications

• Classification: Research Peptide / Lipolytic C-Terminal hGH Fragment (176–191)
• Amino Acid Sequence: Tyr-Leu-Arg-Ile-Val-Gln-Cys-Arg-Ser-Val-Glu-Gly-Ser-Cys-Gly-Phe (Cys7-Cys14 disulfide bridge)
• Form: Sterile lyophilized white powder (cake)
• Component Identification: Verified via Mass Spectrometry (MS) and analytical HPLC
• Recommended Reconstitution Solvent: Sterile bacteriostatic water or sterile phosphate-buffered saline (PBS)
• Storage Conditions: Store long-term at -20 °C in a dry, dark environment. Following reconstitution, keep refrigerated at 2–8 °C in accordance with standard laboratory protocols.

Scientific References & Literature

• Ng, F. M., et al. A growth hormone-derived peptide analogue (AOD9604) stimulates lipolysis and inhibits lipogenesis without diabetogenic effects. Endocrinology, 2000.
• Heffernan, M. A., et al. The effects of human GH and its lipolytic fragment (AOD9604) on lipid metabolism and insulin resistance in cell cultures. American Journal of Physiology-Endocrinology and Metabolism, 2001.
• Wu, Z., et al. The C-terminal region of human growth hormone regulates lipid degradation via non-diabetogenic pathways in adipocyte models. Biochimica et Biophysica Acta, 1993.
• Sato, K., et al. Role of disulfide bond integrity in the conformation and biological potency of C-terminal growth hormone fragments. Peptides, 2004.

Legal Disclaimer & Terms of Purchase

This product is classified and supplied strictly for laboratory, scientific, and in vitro research purposes only (Research Use Only – RUO). This compound is not a drug, medicine, dietary supplement, cosmetic product, or substance intended for human or veterinary consumption, direct administration, injection, or diagnostic procedures.

By placing an order, the purchaser explicitly confirms that they are at least 18 years of age, possess the requisite professional qualifications and laboratory equipment to safely handle research materials, and are fully conversant with all relevant safety protocols for managing research substances. The seller assumes no liability for any use contrary to these terms.