Anti-CD26, clone 202.36 (Monoclonal) [Mouse]

MON1030 reacts with human CD26 (Dipeptidyl peptidase IV), a 110 kDa protein which occurs in the cell membrane of T-lymphocyte and is upregulated after activation. CD26 is also present on endothelial cells and also expressed on activated B-cells and natural killer cells and abundantly on epithelia. CD26 is implicated in a variety of biological functions including T-cell activation, cell adhesion with extracellular matrix such as fibronectin or collagens, and in HIV infection. Crosslinking of CD26 using this antibody dramatically enhances the anti-CD3-induced IL-2 production. In Western blotting, this mAb reacts with only glycosylated CD26, but not with deglycosylated forms. Protein function: Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T- cell activation (PubMed:10951221, PubMed:10900005, PubMed:11772392, PubMed:17287217). Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC (PubMed:10951221, PubMed:10900005, PubMed:11772392, PubMed:14691230). Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (PubMed:17287217). Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion (PubMed:11772392). 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 (PubMed:16651416, PubMed:10593948). May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation (PubMed:18708048). When overexpressed, enhanced cell proliferation, a process inhibited by GPC3 (PubMed:17549790). 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 such as brain natriuretic peptide 32 (PubMed:16254193, PubMed:10570924). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline (PubMed:10593948). [The UniProt Consortium]