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Purely Peptides
Research Catalog

Compound monograph

GIP(1-42)

GIP is a 42-residue endogenous incretin hormone and the native ligand of the GIP receptor.

Published: 2026-09-14Literature/identifier verification: 2026-09-14
GIPGastric inhibitory polypeptideGlucose-dependent insulinotropic peptideIncretin and glucagon receptor ligands

01

Identity & nomenclature

GIP is a 42-residue endogenous incretin hormone and the native ligand of the GIP receptor.

'Gastric inhibitory polypeptide' is the historical name for this same hormone, not a different peptide. Species must stay explicit: human GIP differs from porcine at residues 18 and 34. Full-length GIP must not be merged with GIP(3-42), GIP(1-30)amide, or proGIP — DPP-IV cleavage changes the molecule and its pharmacology. No CAS registry number is recorded. A supplier-supported number was proposed during scoping but was never reconciled to an authoritative registry and does not resolve in PubChem. The PubChem CID recorded here was reached by name and is retained because its molecular formula matches the sequence-derived formula exactly; the name alone would not be sufficient evidence.

Declared aliases and development codes: GIP, Gastric inhibitory polypeptide, Glucose-dependent insulinotropic peptide.

02

Molecular properties

Molecular formulaC226H338N60O66S
Molecular mass4983.6 Da
PubChem CID131954558
UNII1O4H75S7H2
One-letter sequenceYAEGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQ

Forty-two residues, free at both termini. Note residue 1 is TYROSINE — the N-terminal Tyr-Ala distinguishes this hormone from GLP-1's His-Ala and is the single quickest way to tell a GIP-derived scaffold from a GLP-1-derived one.

03

Structural characteristics

Human GIP was isolated from small-intestinal extracts and sequenced by Edman degradation, together with the N-terminally truncated forms GIP(10-42), GIP(11-42) and GIP(17-42). Its N-terminal Tyr-Ala is a DPP-IV substrate; the enzyme releases Tyr-Ala to give GIP(3-42), and the same work identified this as the main degradation route in human serum. Because an intact N-terminus is required for activity in this peptide family, the truncated form is a different substance rather than degraded material of the same one.

04

Molecular targets & mechanisms

Glucose-dependent insulinotropic polypeptide receptor

GIPR

GIPR is a class B G-protein-coupled receptor. The cited discovery and trial records identify it as one of the three receptor relationships declared for retatrutide.

05

Analytical considerations

Require human species, full length and an intact N terminus. A total-GIP assay is not automatically an intact-GIP assay. For any comparison against a GIP-derived analog, retain explicit residue numbering — Ala13, Met14, Ile17 and His18 are positions where off-by-one errors in modification tables are common, because the analogs substitute at several of them.

06

Verified bibliography

  1. The isolation and sequencing of human gastric inhibitory peptide (GIP).

    Moody AJ, Thim L, Valverde I

    FEBS letters · 1984-07-09 · Journal Article

    current
    PMID 6745415DOI 10.1016/0014-5793(84)81114-xGIP(1-42)
  2. Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum.

    Mentlein R, Gallwitz B, Schmidt WE

    European journal of biochemistry · 1993-06-15 · Journal Article

    current
    PMID 8100523DOI 10.1111/j.1432-1033.1993.tb17986.xGLP-1(7-36) amideGIP(1-42)

10

Methodology & citation verification

Reference identity is checked against official PubMed metadata. Local deterministic receipts bind each normalized title and canonical metadata record to its verification date. Scientific values remain absent when an authoritative source has not been verified.

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