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Compound monograph

Human GLP-2(1-33)

Human GLP-2(1-33) is a linear 33-residue peptide with a free amino terminus and a C-terminal carboxyl group. This record describes the unmodified parent covalent structure. Orskov et al. (PMID 2714431) characterize human and pig intestinal GLP-2 as a proglucagon processing product. Horváth et al. (PMID 37528104) place GLP-2 among the gastrointestinal peptides of the glucagon family.

Published: 2026-09-30Last updated: 2026-10-13Literature/identifier verification: 2026-09-30
Also known asGLP-2Glucagon-like peptide-2Human GLP-2hGLP-2

01

Identity & nomenclature

Human GLP-2(1-33) is a linear 33-residue peptide with a free amino terminus and a C-terminal carboxyl group. This record describes the unmodified parent covalent structure. Orskov et al. (PMID 2714431) characterize human and pig intestinal GLP-2 as a proglucagon processing product. Horváth et al. (PMID 37528104) place GLP-2 among the gastrointestinal peptides of the glucagon family.

“GLP-2” on its own specifies neither species nor whether a peptide is intact or shortened, so this record keeps the human (1-33) form explicit. Fragment notation does not specify a preparation’s counterion or hydration state. GSRS UNII 0825W549JC lists primary CAS 223460-79-5 for the free human 33-mer; PubChem CIDs 71300624 and 90488755 encode the same stereospecified structure, with 71300624 selected here.

Canonical name: Human glucagon-like peptide-2 (1-33).

Declared aliases and development codes: GLP-2, Glucagon-like peptide-2, Human GLP-2, hGLP-2.

02

Molecular properties

Molecular formulaC165H254N44O55S
Molecular mass3766.16 Da
CAS Registry Number223460-79-5
PubChem CID71300624
UNII0825W549JC
One-letter sequenceHADGSFSDEMNTILDNLAARDFINWLIQTKITD
Three-letter sequenceHis–Ala–Asp–Gly–Ser–Phe–Ser–Asp–Glu–Met–Asn–Thr–Ile–Leu–Asp–Asn–Leu–Ala–Ala–Arg–Asp–Phe–Ile–Asn–Trp–Leu–Ile–Gln–Thr–Lys–Ile–Thr–Asp
Terminal groupsFree N-terminal amino group; Free C-terminal carboxyl group

Thirty-three residues numbered from His1 to Asp33. Every chiral residue is in the L configuration; Gly4 is achiral.

03

Structural characteristics

The chain runs from His1 to Asp33 with no cysteine, so it has no intramolecular disulfide bond and no covalent macrocycle.

Terminal features: Free N-terminal amino group, Free C-terminal carboxyl group.

04

Molecular targets & mechanisms

05

Analytical considerations

The molecular formula and the 3766.16 Da average mass are calculated from the sequence with CIAAW 2024 abridged atomic weights. Two published average-mass values differ and remain unreconciled: 3769.136 in the PDB entity metadata for entry 2L63, and 3760.0 as the GSRS estimated calculated weight. The sequence rests on Edman, mass-spectrometric and NMR characterization of separate material sets; this is not a lot-specific certificate.

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 ileal peptide extracts in mass-spectrometry and sequencing assays

    Hartmann et al. identified GLP-2 isolated from human ileal extracts as proglucagon residues 126-158 by mass spectrometry and Edman sequencing.

    Reference [1]

  • Rat ileal extracts in HPLC and radioimmunoassays

    Brubaker et al. detected GLP-2-(1-33) and GLP-2-(3-33) in rat ileal extracts, with GLP-2-(3-33) accounting for 16 +/- 7% of total GLP-2 in HPLC and radioimmunoassays.

    Reference [3]

  • Human GLP-2-(1-33) with dipeptidylpeptidase IV

    Brubaker et al. observed liberation of GLP-2-(3-33) when human GLP-2-(1-33) was incubated with dipeptidylpeptidase IV in an enzyme-cleavage assay.

    Reference [3]

  • Gly2-substituted human GLP-2 with dipeptidylpeptidase IV

    Brubaker et al. observed that replacing Ala2 with Gly2 prevented dipeptidylpeptidase-IV cleavage of human GLP-2 in an enzyme-cleavage assay.

    Reference [3]

  • Pig and human small-intestinal extracts in radioimmunoassays

    Orskov et al. detected no GLP-2-associated signal in the PG 151-160 radioimmunoassay after gel filtration of pig and human small-intestinal extracts.

    Reference [4]

Animal studies

  • Rats in a plasma radioimmunoassay study

    Brubaker et al. measured a 3.6-fold increase in total plasma immunoreactive GLP-2 in fed rats relative to fasted rats (P < 0.001) by radioimmunoassay.

    Reference [3]

06

Verified bibliography

Cited studies by type

The 5 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

    Structure, measurement, and secretion of human glucagon-like peptide-2.

    Hartmann B, Johnsen AH, Orskov C, Adelhorst K, Thim L, Holst JJ

    Peptides · 2000-01 · Journal Article

    current
    PMID 10704722DOI 10.1016/s0196-9781(99)00176-xHuman GLP-2(1-33)

  2. Reference 2

    Conformational and molecular interaction studies of glucagon-like peptide-2 with its N-terminal extracellular receptor domain.

    Venneti KC, Hewage CM

    FEBS letters · 2010-12-15 · Journal Article

    current
    PMID 21167157DOI 10.1016/j.febslet.2010.12.011Human GLP-2(1-33)

  3. Reference 3

    Circulating and tissue forms of the intestinal growth factor, glucagon-like peptide-2.

    Brubaker PL, Crivici A, Izzo A, Ehrlich P, Tsai CH, Drucker DJ

    Endocrinology · 1997-11 · Journal Article

    current
    PMID 9348213DOI 10.1210/endo.138.11.5482Human GLP-2(1-33)

  4. Reference 4

    Carboxypeptidase-B-like processing of the C-terminus of glucagon-like peptide-2 in pig and human small intestine.

    Orskov C, Buhl T, Rabenhøj L, Kofod H, Holst JJ

    FEBS letters · 1989-04-24 · Journal Article

    current
    PMID 2714431DOI 10.1016/0014-5793(89)81332-8Human GLP-2(1-33)

  5. Reference 5

    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
Hartmann B et al. 2000Study models reported: in vitro · from the abstract
Venneti KC et al. 2010Chemical, structural or analytical study; no biological model reported
Brubaker PL et al. 1997Study models reported: in vitro; animal (rat) · from the abstract
Orskov C et al. 1989Study models reported: in vitro · from the abstract
Horváth D et al. 2023Chemical, structural or analytical study; no biological model reported

Record history

Published 2026-09-30.

  • : 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. Human GLP-2(1-33). Published 2026-09-30; updated 2026-10-13. https://purelypeptides.org/research/compounds/glp-2/

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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