HGH 176-191 5 mg

HGH 176-191, also referred to as HGH Fragment 176-191, is a synthetic 16-residue hexadecapeptide corresponding to the C-terminal region (residues 176 to 191) of human growth hormone. It is supplied as an investigational laboratory peptide for receptor-independent metabolic-pathway research and structure-activity studies that examine how a discrete C-terminal domain of human growth hormone engages adipocyte signaling pathways distinct from the growth-hormone-receptor engagement profile of the intact 191-residue molecule.

Laboratory research studies have positioned HGH 176-191 as a reference compound for examining domain-specific peptide engagement of adipocyte signaling cascades. Research models have characterized its modulation of cyclic-AMP signaling, downstream protein-kinase-A activation, and the resulting engagement of hormone-sensitive-lipase and lipogenic-enzyme pathways in adipocyte research models, providing comparative data versus full-length recombinant human growth hormone and other C-terminal fragment analogs such as AOD-9604 (Ng & Bornstein, 1978, American Journal of Physiology).

Beyond adipocyte pathway research, HGH 176-191 is investigated in cellular and animal research models that explore receptor-independent peptide engagement, β3-adrenergic-receptor expression modulation, structure-activity relationships within the C-terminal domain of human growth hormone, and comparative pharmacology versus intact recombinant human growth hormone. Because the 176-191 fragment lacks the receptor-dimerization domains of the full-length molecule, it is a frequent subject of research investigating how isolated peptide domains engage downstream metabolic pathways without engaging the canonical growth-hormone-receptor pathway.

The peptide is supplied as a lyophilized powder to ensure optimal stability during storage and handling.

Human growth hormone is a 191-residue protein hormone secreted by pituitary somatotroph cells that engages the growth-hormone receptor and participates in somatotropic-axis research. Early structure-activity research on synthetic C-terminal fragments of human growth hormone demonstrated that discrete peptide domains within the full-length molecule could engage distinct metabolic signaling pathways in research models, independent of the receptor-dimerization domains required for canonical growth-hormone-receptor engagement.

HGH 176-191 was identified through this structure-activity research as a 16-residue C-terminal hexadecapeptide that retains adipocyte-pathway engagement in research models while lacking the structural features required for growth-hormone-receptor activation. The 176-191 sequence, Tyr-Leu-Arg-Ile-Val-Gln-Cys-Arg-Ser-Val-Glu-Gly-Ser-Cys-Gly-Phe, includes an internal disulfide bridge between Cys182 and Cys189 that stabilizes the fragment's secondary structure in research models.

This receptor-independent engagement profile has made HGH 176-191 a widely studied reference compound for laboratory investigations of adipocyte cyclic-AMP signaling, β3-adrenergic-receptor expression modulation, lipogenic-enzyme pathway research, and comparative pharmacology versus full-length recombinant human growth hormone. Research interest spans adipocyte signaling models, structure-activity studies on growth-hormone fragments, and comparative research with related C-terminal analogs such as AOD-9604.

HGH 176-191 Structure

1. Receptor-Independent Adipocyte Pathway Engagement

HGH 176-191 engages adipocyte signaling pathways in research models without engaging the canonical growth-hormone receptor, because the 16-residue C-terminal fragment lacks the receptor-dimerization domains of the intact 191-residue molecule. Research models have characterized this receptor-independent engagement profile as a distinguishing feature versus full-length human growth hormone (Ng & Bornstein, 1978, AJP).

2. Modulation of Cyclic AMP and Protein Kinase A

Upon engagement of adipocyte signaling pathways, HGH 176-191 modulates intracellular cyclic AMP accumulation. Downstream, this is associated with protein kinase A activation and phosphorylation of hormone-sensitive lipase, both of which are extensively studied in adipocyte research as upstream regulators of lipid-pathway engagement in research models.

3. β3-Adrenergic-Receptor Expression Modulation

Laboratory research studies have characterized HGH 176-191 as modulating β3-adrenergic-receptor expression in adipocyte research models. Comparative studies in β3-AR-knockout research models have investigated the extent to which the fragment's metabolic-pathway engagement requires β3-AR signaling versus alternative receptor-independent mechanisms, with research models indicating contributions from both pathways.

4. Engagement of Lipogenic-Enzyme Pathways

In addition to engaging lipid-mobilization pathways, HGH 176-191 modulates the expression of lipogenic enzymes including acetyl-CoA carboxylase in adipocyte research models. This dual engagement, modulation of both lipid-mobilization and lipogenic-enzyme pathways, is an active area of structure-activity research on the C-terminal domain of human growth hormone.

Research Applications

Conclusion

HGH 176-191 represents a structurally defined C-terminal hexadecapeptide of human growth hormone that has become a reference compound in receptor-independent metabolic-pathway research. Its 16-residue sequence retains adipocyte-pathway engagement in research models while lacking the receptor-dimerization domains required for canonical growth-hormone-receptor engagement, making it a valuable investigational laboratory peptide for studying domain-specific peptide pharmacology, structure-activity relationships within the C-terminal region of human growth hormone, and comparative engagement of cyclic-AMP and β3-adrenergic-receptor pathways in adipocyte research models.

Research Use Disclaimer

This product is intended for research and laboratory use only. It is designed exclusively for in vitro research purposes. All information provided is for educational and research reference only. This product is not intended for human or animal use. It is not a drug, food, or cosmetic and must not be marketed, labeled, or used as such. Use and handling are restricted to trained and qualified professionals.