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 α/β hydrolase domain and an eight-bladed β-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.
|InnoZyme™ DPP IV Activity Assay Kit||CBA097|
|InnoZyme™ DPP IV Immunocapture Activity Assay||CBA085|
|Dipeptidyl Peptidase IV (CD26), Porcine Kidney||317640|
|Dipeptidylpeptidase IV, His•Tag®, Human, Recombinant, S. frugiperda||317639|
|Dipeptidylpeptidase IV, Human Placenta||317630|
|Dipeptidylpeptidase IV Substrate I, Fluorogenic||125510|
|Dipeptidylpeptidase IV Inhibitor I||416200|