>Dipeptidyl Peptidase (DPP)
Dipeptidyl Peptidase (DPP)
Dipeptidyl peptidases (DPPs) is a subclass of exopeptidases that includes enzymes which cleave two amino acids from the end of a peptide chain. They are linked to a variety of diseases including type 2 diabetes, obesity and cancer.
Sino Biological offers a comprehensive set of tools for dipeptidyl peptidase related studies, including recombinant proteins, antibodies (rabbit mAbs, mouse mAbs, rabbit pAbs), ELISA kits, and ORF cDNA clones.
Dipeptidyl Peptidase (DPP) Products
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Dipeptidyl Peptidase (DPP) Background
Dipeptidyl peptidases (DPPs) is a subclass of exopeptidases that includes enzymes which cleave two amino acids from the end of a peptide chain. They are linked to a variety of diseases including type 2 diabetes, obesity and cancer. Members of dipeptidyl peptidase include cathepsin C(DPP1), DPP3, DPP4, DPP6, DPP7, DPP8, DPP9 and DPP10.
Cathepsin C may play a central role in the activation of many serine proteases in immune/inflammatory cells. It catalyses excision of dipeptides from the N-terminus of protein and peptide substrates. Defects in cathepsin C can cause Papillon-Lefevre disease, an autosomal recessive disorder characterized by palmoplantar keratosis and periodontitis.
DPP4 is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. It is involved in immune regulation, signal transduction and apoptosis. DPP4 also plays a major role in glucose metabolism. It is responsible for the degradation of incretins such as GLP-1.
DPP3, DPP6, DPP8, DPP9 and DPP10 are members of the S9B family. A S9B family is a small family of dipeptidyl peptidases that are able to cleave peptide substrates at a prolyl bond. DPP3 has post-proline dipeptidyl aminopeptidase activity and binds a single zinc ion with its zinc-binding motif. Increased activity of this protein is related to endometrial and ovarian cancers.
Dipeptidyl Peptidase (DPP) Related Studies
- Kar NC, et al. (1978) Dipeptidyl peptidases in human muscle disease. Clin Chim Acta. 82(1-2): 185-92.
- Vanha-Perttula T. (1989) Dipeptidyl peptidase III and alanyl aminopeptidase in the human seminal plasma: origin and biochemical properties. Clin Chim Acta. 177(2):179-95.
- Shimamori Y, et al. (1989) Human placental dipeptidyl aminopeptidase III: hydrolysis of enkephalins and its stimulation by cobaltous ion. Biochem Med Metab Biol. 40(3):305-10.