CD26/Dipeptidyl Peptidase 4 Protein, Cynomolgus/Rhesus macaque (HEK293)

Dipeptidyl peptidase 4 (DPP4), also known as T cell surface antigen CD26, is a ubiquitous enzyme in human. It is widely expressed in a variety of tissues (lung, brain, pancreas, kidney, blood vessels, prostate, uterus, thymus, lymph nodes and spleen) and many cells (epithelial cells, inner skin cells, immune cells), especially highly expressed in kidney and small intestine. It is a transmembrane glycoprotein composed of 766 amino acids with a relative molecular weight of 110kDa. Its basic structure mainly includes: intracellular N-terminal region, transmembrane region and extracellular region. The extracellular part consists of a flexible rod, a glycosylation rich region (binding region with anti-CD26 antibody, adenosine deaminase (ADA) and caveolin-1), a cysteine rich region (binding region with collagen and fibronectin) and a catalytic region composed of the catalytic triad Ser630, Asp708 and His740. DPP4 contains nine potential glycosylation sites for glycosylation modification. Among them, co-translational core N-glycosylation was significantly associated with DPP4 folding and stability, whereas N-terminal sialylation appeared to regulate more pathophysiological processes. Hypersialylated DDP4 is responsible for the development of HIV and rheumatoid arthritis, while undersialylated DPP4 is shown to be linked with lung cancer^[1].