Dipeptidyl peptidase 4 (DPP-4), also known as CD26, is a type II transmembrane glycoprotein with a major role in glucose metabolism.1 It is composed of a short cytoplasmic tail, a transmembrane domain, and a large extracellular domain, which contains a flexible stalk, glycosylation- and cysteine-rich regions, and a catalytic region. DPP-4 is expressed in endothelial and epithelial tissues, as well as T cells, activated B cells, activated natural killer (NK) cells, and myeloid cells. It functions as a homodimer that cleaves X-proline dipeptides from the N-terminus of various polypeptide substrates, such as GLP-1, to regulate glucose metabolism, immune responses, nociception, and blood pressure.1,2,3 Additionally, DPP-4 acts as a co-stimulator of T cell receptor-mediated T cell activation and functional receptor for Middle East respiratory syndrome coronavirus (MERS-CoV).1,4 Small molecule-induced inhibition of DPP-4 improves glucose tolerance in animal models of insulin resistance and has antihypertensive effects in various rodent models of hypertension.2,3 Cayman's DPP-4/CD26 Extracellular Domain (human, recombinant) protein can be used for binding assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of DPP-4 (amino acids 29-766) fused to His-tagged human IgG1 Fc at its N-terminus, consists of 975 amino acids and has a calculated molecular weight of 112 kDa. As a result of glycosylation, the monomer migrates at approximately 120-130 kDa by SDS-PAGE under reducing conditions.WARNING This product is not for human or veterinary use.
