Anti-CD26 Monoclonal Antibody (Clone:BA5b)

CD26, also known as dipeptidyl peptidase IV (DPP-IV), is a homodimeric cell surface serine peptidase that degradates IFN-gamma-induced cytokines, acts as a T cell costimulatory molecule, and participates in multiple immunopathological roles in leukocyte homing and inflammation. Alterations in its peptidase activity are characteristic of malignant transformation. The enzymatic activity increases dramatically with tumour grade and severity. CD26 is expressed in various blood cell types, but also e.g. in cells that are histogenetically related to activated fibroblasts. Alterations in CD26 density have been reported on circulating monocytes and CD4+ T cells during rheumatoid arthritis and systemic lupus erythematosus. 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]