Anti-CD26, clone 134-2C2

1 mg/ml in sterile PBS, BSA free, sodium azide free. Recognizes a glycoprotein of 110kDa, identified as CD26. It is an atypical serine protease belonging to the prolyl oligopeptidase family. It is expressed on lymphocyte cells and is upregulated during T-cell activation. CD26 is 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. 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]