Lot certificates published
Plain, secure packaging
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. Horváth et al. (PMID 37528104) place GIP among the gastrointestinal peptides of the glucagon family.

Published: 2026-09-14Last updated: 2026-10-14Literature/identifier verification: 2026-09-14
Also known asGIPGastric inhibitory polypeptideGlucose-dependent insulinotropic peptide
Incretin and glucagon receptor ligands

01

Identity & nomenclature

GIP is a 42-residue endogenous incretin hormone and the native ligand of the GIP receptor. Horváth et al. (PMID 37528104) place GIP among the gastrointestinal peptides of the glucagon family.

'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. GSRS UNII 1O4H75S7H2 assigns primary CAS 100040-31-1 to the human 42-residue free peptide, while PubChem CID 131954558 matches its connectivity and formula but leaves all 46 atom stereocentres undefined.

Canonical name: Glucose-dependent insulinotropic polypeptide.

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

02

Molecular properties

Molecular formulaC226H338N60O66S
Molecular mass4983.6 Da
CAS Registry Number100040-31-1
PubChem CID131954558
UNII1O4H75S7H2
One-letter sequenceYAEGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQ
Terminal groupsFree N-terminus; Free C-terminal carboxyl

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.

Terminal features: Free N-terminus, Free C-terminal carboxyl.

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.

Disagreements and mix-ups

Points where sources disagree about this compound's identity, or where a name or form is easily confused with another, as noted in this record. The discrepancy register quotes the passage for each one.

What the studies reported

Each finding describes one cited study in its stated model. These observations are specific to that study and do not establish effects in other settings.

Cell and tissue studies

  • Human small-intestinal peptide extracts

    Moody et al. reported isolation of human GIP 1-42 from acid-ethanol extracts of human small intestine and established its full sequence by Edman degradation.

    Reference [1]

  • Purified human placental dipeptidyl-peptidase IV assay

    Mentlein et al. reported hydrolysis of GIP to its des-Tyr-Ala derivative by dipeptidyl-peptidase IV purified from human placenta.

    Reference [2]

  • Human serum degradation assay

    Mentlein et al. identified des-Tyr-Ala GIP and Tyr-Ala as major degradation products in human serum incubations, and dipeptidyl-peptidase IV inhibitors completely abolished production of these fragments.

    Reference [2]

06

Verified bibliography

Cited studies by type

The 3 papers this record cites, counted by the kind of work each reports. A count is the size of this record's selection, not of the research that exists, and says nothing about results, safety, effectiveness or approval.

A paper can report more than one kind of work. Each count opens those papers in the bibliography. Compare every record on the Evidence Map.

  1. Reference 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. Reference 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)

  3. Reference 3

    Polymorphic amyloid nanostructures of hormone peptides involved in glucose homeostasis display reversible amyloid formation.

    Horváth D, Dürvanger Z, K Menyhárd D, Sulyok-Eiler M, Bencs F, Gyulai G, Horváth P, Taricska N, Perczel A

    Nature communications · 2023-08-01 · Journal Article

    current
    PMID 37528104PMC10394066DOI 10.1038/s41467-023-40294-xGIP(1-42)GlucagonGLP-1(7-36) amideGLP-1(7-37)Human GLP-2(1-33)Exenatide

Study models of these references

What kind of experiment each cited paper reports, taken from its abstract unless marked. Not a summary of results.

ReferenceStudy models
Moody AJ et al. 1984Study models reported: in vitro · from the abstract
Mentlein R et al. 1993Study models reported: in vitro · from the abstract
Horváth D et al. 2023Chemical, structural or analytical study; no biological model reported

Record history

Published 2026-09-14.

  • : Sequence and structure
  • : Identity and nomenclature
  • : Identity and nomenclature, References

Each entry names the parts of this record that changed on that date. Changes to links between records and to catalogue links are not listed. This history covers the tracked record fields; study findings are not listed here.

Cite this record: Purely Peptides Research Library. GIP(1-42). Published 2026-09-14; updated 2026-10-14. https://purelypeptides.org/research/compounds/gip-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.

Read the full methodology →