Anti-Rat CD26 (clone: 5E8)

Dipeptidyl peptidase IV (DPP IV) is widely distributed in a number of mammalian tissues and is suggested to play an important role in various kinds of biological processes. DPP IV (CD26) is a serine-type protease that removes the amino-terminal dipeptide from peptide substrate provided that the penultimate amino acid residue is proline or alanine. DPP IV plays an important role in the reclamation of peptide nitrogen from larger peptides. The monoclonal antibody 5E8 reacts with DPP IV present on the apical surface of epithelial cells in the pancreas, small intestine, colon, and bile duct. Furthermore antibody 5E8 reacts with DPP IV on the laminar portions of the proximal renal tubule cells, and, weakly, on the glomeruli. Protein function: Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF- kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. [The UniProt Consortium]