Glucagon - Like Peptide 1, GLP - 1 (7 - 36), amide, human

Glucagon-like peptide-1 (GLP-1) is derived from the transcription product of the proglucagon gene. The major source of GLP-1 in the body is the intestinal L cell that secretes GLP-1 as a gut hormone; Glucagon-like peptide 1 (GLP-1) is a potent stimulator of glucose-dependent insulin release and plays important roles on gastric motility and the suppression of plasma glucagon levels; The biologically active forms of GLP-1 are: GLP-1-(7-37) and GLP-1-(7-36)NH2. Those peptides result from selective cleavage of the proglucagon molecule.

Glucagon - Like Peptide 1, GLP - 1 (7 - 36), amide, human is a synthetic research peptide in the glucagon-like peptide-1 (GLP-1) research peptide family. GLP-1 is an incretin peptide that activates the class B GLP-1 receptor. Structure-activity studies using substituted and truncated GLP-1 peptides demonstrated that defined residues contribute to receptor binding and cyclic-AMP signaling, while structural studies show a helical peptide conformation within the activated receptor complex. Modified GLP-1 variants are therefore useful for separating receptor binding from receptor activation and for comparing analog potency.

• GLP-1 receptor binding assays
• cAMP and receptor-signaling experiments
• incretin peptide structure-activity studies
• agonist/antagonist comparisons
• analytical peptide reference applications

For fragments, substituted analogs, labeled peptides, stereochemical variants, or terminally modified forms, experimental behavior should be evaluated for the exact construct rather than assumed to match the native parent peptide. Sequence-dependent solubility, aggregation, adsorption, oxidation, and stability should be considered when establishing reconstitution, storage, and assay conditions.

1. Structure-activity relationships of glucagon-like peptide-1(7-36)amide
2. Crystal structure of the GLP-1 receptor bound to a peptide agonist