HGH Fragment 176-191

HGH Fragment 176-191 is the synthetic 16-residue C-terminal segment of human growth hormone, beginning with phenylalanine.

Identity

Sequence

H-FLRIVQCRSVEGSCGF-OH

Residues

16

Bridges and complexes

Cys7–Cys14 (S–S)

Molecular formula

C₇₈H₁₂₃N₂₃O₂₂S₂

Average molecular weight

1799.1 g/mol

Monoisotopic mass (calculated)

1797.8654 Da

CAS number

66004-57-7

PubChem CID

172966177

Other names

Somatotropin (176-191) · hGH (176-191)

The values refer to the free peptide. PubChem also has an acetic acid-containing record, with formula C80H127N23O24S2 and mass 1859.1 g/mol; those values are excluded here. CAS comes from the somatotropin fragment record. No separate UniProt identity was verified; the sequence represents the structure, without atom coordinates, SMILES or blend components.

Identity data from: PubChem CID 172966177 · PubChem CID 16131230 CAS record · PubChem CID 172966176 annotated peptide sequence, excluding acetic acid

Research overview

HGH Fragment 176-191 corresponds to the last 16 residues of mature human growth hormone. The sequence FLRIVQCRSVEGSCGF begins with phenylalanine, ends with a free carboxyl group and contains the Cys7–Cys14 disulfide bridge represented in the identity data. An early fragment-comparison study included this segment alongside several neighbouring C-terminal sequences. The positional name therefore identifies a defined part of the parent hormone rather than the entire protein [1].

The early work used normal rats and compared synthetic fragments spanning residues 172-191, 176-191, 177-191, 178-191, 179-191 and 180-191. This comparison placed sequence boundaries and physical configuration at the centre of the experimental question. The authors discussed the requirement for an appropriate configuration of the peptide sequence. These were experiments on related fragments in a specified animal system; their interpretation requires keeping the individual molecular identities separate [1].

A later paper examined mechanisms associated with synthetic peptides related to the same C-terminal region. PubMed indexes both somatotropin (176-191) and somatotropin (177-191), together with rat models, for that record. Its public entry has no abstract, so detailed experimental findings or a specific receptor assignment are not attributed here. The citation establishes a separate strand of fragment research, with a different publication and evidentiary scope [2].

Laboratory storage and handling

Store sealed peptide vials under the temperature conditions stated in the lot documentation, protected from light and moisture. Let a cold vial reach room temperature before opening to limit condensation. Avoid repeated freezing and thawing of laboratory stocks, record storage history and the lot identifier, and use standard laboratory protective equipment. Chemical modifications and counterions should be checked against the supplied analytical description.

Questions about HGH Fragment 176-191

References

1. Hyperglycemic action of synthetic C-terminal fragments of human growth hormone. Am J Physiol 1978. PMID 645904
2. The mechanism of the hyperglycaemic action of synthetic peptides related to the C-terminal sequence of human growth hormone. Biochim Biophys Acta 1982. PMID 6810951

Identity data checked on 2026-10-03. Literature summaries describe published research models and are not specifications of any product lot.