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

• DPP1
• DPP4
• DPP9
• DPP3
• DPP7 / DPP2
• DPP10

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

1. Kar NC, et al. (1978) Dipeptidyl peptidases in human muscle disease. Clin Chim Acta. 82(1-2): 185-92.
2. 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.
3. 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.