Glucagon (1 - 29), bovine, human, porcine

Glucagon is a 29-amino acid peptide hormone secreted by pancreatic α-cells that raises blood glucose and (indirectly) insulin levels. Glucagon acts via a G protein-coupled receptor, which results in the release of glucose 1-phosphate from glycogen.. Glucagon-(19-29) is 1000-fold more potent that glucagon as an inhibitor of the liver plasma membrane calcium pump, which suggests that this peptide fragment is naturally occurring. Since glucagon-(19-29) is undetectable in plasma, the processing of glucagon into its (19-29) fragment may occur upon interaction of glucagon with its target tissues.

Glucagon (1 - 29), bovine, human, porcine is a synthetic research peptide in the glucagon research peptide family. Glucagon is a 29-residue peptide hormone and the endogenous ligand of the glucagon receptor, a class B G-protein-coupled receptor. Structural work with glucagon analogs supports the two-domain recognition model in which peptide contacts with the extracellular and transmembrane receptor regions cooperate in ligand binding and activation. Truncated, substituted, amidated, and labeled glucagon peptides are useful for defining receptor-contact residues and distinguishing binding from signaling.

• glucagon receptor binding assays
• cAMP signaling studies
• glucagon structure-activity analysis
• peptide/receptor interaction studies
• analytical 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 of the glucagon receptor in complex with a glucagon analogue
2. Roles of specific extracellular domains of the glucagon receptor in ligand binding and signaling