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G418/Hygromycin B Promo

Reagents for DPP IV Research

Dipeptidyl peptidase IV (DPP IV), a widely distributed, multifunctional transmembrane serine protease, has attracted considerable interest in recent times. It modulates the activity of several peptide hormones by cleaving Xaa-Pro or Xaa-Ala from their NH2-terminal. DPP IV functions as a dimer and each monomeric subunit has an a/b hydrolase domain and an eight-bladed b-propeller domain. Both these domains participate in inhibitor binding at the active site. Of considerable interest is the cleavage of glucagon-like peptide-1 (GLP-1) by DPP IV.

GLP-1 is shown to be important in maintaining glucose homeostasis. It blocks glucagon secretion, delays gastric emptying, and stimulates insulin biosynthesis. GLP-1 has been under consideration as an alternate treatment for type II diabetes. However, its short half-life (<1 min) severely limits its use as a treatment option. To overcome this difficulty, inhibition DPP IV has been proposed as a viable option and DPP IV inhibitors are shown to improve glucose tolerance in animal models of type II diabetes.

Assay Kits


Enzymes


Antibody


Substrate


Inhibitor