Scientific Background | Cysteine-GLP-1 (1-37) (human, bovine, guinea pig, mouse, rat) 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. |
Experimental Notes | 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. |
