GLP-1/Glucagon-Like Peptide, human

GLP-1/Glucagon-Like Peptide, human is a 37-residue synthetic peptide (H-His-Asp-Glu-Phe-Glu-Arg-His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys-Glu-Phe-Ile-Ala-Trp-Leu-Val-Lys-Gly-Arg-Gly-OH, trifluoroacetate salt) representing the full-length proglucagon-derived GLP-1 peptide, also designated GLP-1(1-37)-OH. It includes all six upstream N-terminal residues (His-Asp-Glu-Phe-Glu-Arg) preceding the bioactive core and terminates as a free acid at Gly-37, rather than the C-terminal amide found in GLP-1(7-36)-NH2. This represents the unprocessed, glycine-extended, full-length proglucagon reading frame before both N-terminal truncation by PC1/3 and C-terminal amidation.

Proglucagon processing in intestinal L cells generates GLP-1 by PC1/3-catalyzed cleavage at the N-terminal side of His7 and by peptidylglycine alpha-amidating monooxygenase (PAM) converting the C-terminal Gly-OH to the amidated Arg-NH2 of the bioactive 7-36-NH2 form. The dual processing steps — N-terminal truncation and C-terminal amidation — are both required to generate the highest-potency GLP-1R agonist form. Mojsov and colleagues' discovery of GLP-1(7-37) as an insulinotropic incretin established that the truncation at His7 was essential for receptor engagement, and subsequent fragment comparison work (Suzuki S et al., Endocrinology, 1989, PMID 2684616) systematically mapped which N-terminal and C-terminal extensions reduced activity — findings that place the full-length 1-37 glycine-acid form as the pharmacological starting point from which both processing events converge on the active drug-like sequence. GLP-1R expression cloning confirmed the structural framework for receptor selectivity (Thorens B, Proc Natl Acad Sci USA, 1992, PMID 1326760).

Potential Research Applications: - Proglucagon processing enzymology: PC1/3 cleavage kinetics (N-terminal maturation) and PAM amidation (C-terminal activation) - Structural and comparative pharmacology reference for full-length vs. truncated GLP-1 forms - Mass spectrometry method development for intact proglucagon-derived peptide analysis - Immunoassay cross-reactivity mapping: full-length vs. active GLP-1 antibody discrimination

Market Context: This full-length free-acid GLP-1 precursor form is currently stocked by a single supplier on this platform (CPC Scientific) at approximately $104.50/mg, consistent with its specialized use as a processing-enzymology reference standard.

Cited Research: Suzuki S et al. (1989). Comparison of the effects of various C-terminal and N-terminal fragment peptides of glucagon-like peptide-1 on insulin and glucagon release from the isolated perfused rat pancreas. Endocrinology. PMID 2684616. Thorens B (1992). Expression cloning of the pancreatic beta cell receptor for the gluco-incretin hormone glucagon-like peptide 1. Proc Natl Acad Sci USA. PMID 1326760.

Note: the cited literature establishes the processing requirements that define why this full-length 1-37 free-acid sequence is a structural precursor reference rather than an active GLP-1R agonist.

For laboratory research use only. Not for human or veterinary use, diagnosis, treatment, cure, or prevention of any disease. THIS PRODUCT IS NOT FOR HUMAN CONSUMPTION.