DPP4/CD26, Human

USA

-80

Dipeptidyl peptidase-4 (DPP4), also known as adenosine deaminase complexing protein 2 or CD26 (cluster of differentiation 26), is an antigenic enzyme expressed on the surface of most cell types and is associated with immune regulation, signal transduction and apoptosis. It is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. DPP4 is related to attractin, FAP, DPP8 and DPP9. DPP4 plays a major role in glucose metabolism. It is responsible for the degradation of incretins such as GLP-1. DPP4 plays an important role in tumor biology, and is useful as a marker for various cancers, with its levels either on the cell surface or in the serum increased in some neoplasms and decreased in others. DPP-4 binds the enzyme adenosine deaminase specifically and with high affinity, however the significance of this interaction has yet to be established.
Recombinant Human DPP4/CD26 produced in CHO cells is a polypeptide chain containing 744 amino acids. A fully biologically active molecule, rhDPP4/CD26 has a molecular mass of 110 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.