Glucagon-Like Peptide (GLP) I (7-36), amide, human (Human GLP-1-(7-36)-amide) is a physiological incretin hormone that stimulates insulin secretion. In Vitro: The sequence of Glucagon-Like Peptide after residue 7 shows similarities to glucagon and to other biologically active members of the secretin peptide family, particularly glucose-dependent insulinotropic peptide (GIP). This sequence has been especially well preserved, showing 66% nucleotide homology with GLP-1 in the proglucagon of the very primitive anglerfish. This 7-36 sequence of GLP-1 is a potent insulin-releasing peptide in vitro^[1]. Glucagon-Like Peptide (GLP) I (7-36), amide is a product of the tissue-specific post-translational processing of the glucagon precursor. It is released postprandially from intestinal endocrine L cells and stimulates insulin secretion. DPP IV is the main degradation enzyme for GLP-l(7 - 36)amide in human serum. Dipeptidyl-peptidase IV can initiate the metabolism of GIP and GLP-1(7-36)amide in human serum^[2]. In Vivo: Glucagon-Like Peptide (GLP) I (7-36), amide is a physiological incretin hormone that is released after nutrient intake from the lower gut and stimulates insulin secretion at elevated plasma glucose concentrations. Exogenous GLP-1 (7-36 amide) is an effective means of normalizing fasting plasma glucose concentrations in poorly-controlled Type 2 diabetic subjects^[3]. Exogenously administered GLP-1-(7–36)amide is extremely labile in vivo, with more than 80% being cleaved into GLP-1-(9–36)amide after sc or iv administration^[4].