HRP Conjugated Human DPP4 / CD26 Recombinant Rabbit Monoclonal Antibody [PSH19-27] - Detector

功能

Dipeptidyl peptidase-4 (DPP4 or DPPIV), also known as adenosine deaminase complexing protein 2 or CD26 (cluster of differentiation 26) is a protein that, in humans, is encoded by the DPP4 gene. DPP4 is related to FAP, DPP8, and DPP9. The enzyme was discovered in 1966 by Hopsu-Havu and Glenner, and as a result of various studies on chemism, was called dipeptidyl peptidase IV [DP IV]. The protein encoded by the DPP4 gene is an enzyme expressed on the surface of most cell types and is associated with immune regulation, signal transduction, and apoptosis. It is a type II transmembrane glycoprotein, but a soluble form, which lacks the intracellular and transmembrane part, is present in blood plasma and various body fluids. DPP-4 is a serine exopeptidase that cleaves X-proline or X-alanine dipeptides from the N-terminus of polypeptides. Peptide bonds involving the cyclic amino acid proline cannot be cleaved by the majority of proteases and an N-terminal X-proline "shields" various biopeptides.[7] Extracellular proline-specific proteases therefore play an important role in the regulation of these biopeptides. DPP-4 is known to cleave a broad range of substrates including growth factors, chemokines, neuropeptides, and vasoactive peptides. The cleaved substrates lose their biological activity in the majority of cases, but in the case of the chemokine RANTES and neuropeptide Y, DPP-4 mediated cleavage leads to a shift in the receptor subtype binding.

背景文献

1. Love KM et al. DPP4 Activity, Hyperinsulinemia, and Atherosclerosis. J Clin Endocrinol Metab. 2021 May

2. Chen SY et al. DPP4 as a Potential Candidate in Cardiovascular Disease. J Inflamm Res. 2022 Sep

亚细胞定位

Secreted, Cell membrane, Apical cell membrane, invadopodium membrane, lamellipodium membrane, Cell junction, Membrane raft.

UNIPROT

SwissProt: P27487 Human

别名