Glucagon-like peptide 1 (GLP-1) is a 3.5 kD incretin hormone secreted primarily from the enteroglucagon-producing L-cells in the small intestine. It is released in response to a meal and is highly potent in stimulating insulin and inhibiting glucagons secretion. GLP-1 (7-36) amide and GLP-1 (7-37) are the biologically active forms of GLP-1. In vivo, the active forms are rapidly degraded by the dipeptidyl peptidase IV (DPP-IV).

GLP-1 (7-36) amide is an incretin hormone that causes glucose dependent release of insulin by pancreatic beta cells. It is the cleavage product of GLP-1 (1-36) amide peptide. Both GLP-1 (7-36) and GLP-1 (7-37), also play roles in gastric motility (gastric emptying), on the suppression of plasma glucagon levels (glucose production) and possibly on the promotion of satiety and stimulation of glucose disposal in peripheral tissues independent of the actions of insulin. GLP-1 (7-36) has a short half life of less than 2 minutes, and like GIP, is rapidly degraded by the enzyme dipeptidyl peptidase IV (DPP-4), which is widely expressed in a number of sites, including the endothelial cells of small gut arterioles. DPP-4 degrades GLP-1 (7-36) into the non insulinotropic GLP-1 (9-36)

The GLP-1 (x-36) amide Kit provides assay-specific components for the quantitative determination of both natural and recombinant glucagon-like peptide-1 (GLP-1) amidated isoforms in serum, plasma, and tissue culture supernatant. The assay recognizes GLP1 (1-36)amide, GLP-1 (7-36)amide, and GLP-1 (9-36)amide. The GLP-1 protein sequence is 100% conserved across all species.