DPP-4/CD26 Extracellular Domain (human, recombinant)

ADABP|ADCP2|Adenosine Deaminase Complexing Protein 2|Dipeptidyl Peptidase 4|DPP-IV|T-cell Activation Antigen CD26|TP103

Dipeptidyl peptidase 4 (DPP-4), also known as CD26, is a type II transmembrane glycoprotein with a major role in glucose metabolism.{54903} 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.{54903,54904,54905} 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).{54903,54906} 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.{54904,54905} 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.

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-80

Lyophilized from sterile PBS, pH 7.4

365

≥95% estimated by SDS-PAGE