Mouse CD26/DPP4 ELISA Kit PicoKine®

Mouse CD26/DPP4 ELISA Kit PicoKine® (96 Tests). Quantitate Mouse Dpp4 in cell culture supernatants, cell lysates, serum and plasma (heparin, EDTA). Sensitivity: 10pg/ml.

Dipeptidyl peptidase-4 (DPP4), also known as adenosine deaminase complexing protein 2 or CD26 (cluster of differentiation 26) is a protein that, in humans, is encoded by the DPP4 gene. By fluorescence in situ hybridization, the CD26 gene was mapped to 2q24.3. DPP4 plays a major role in glucose metabolism. It is responsible for the degradation of incretins such as GLP-1. Furthermore, it appears to work as a suppressor in the development of cancer and tumours. CD26/ DPP4 plays an important role in tumor biology, and is useful as a marker for various cancers, with its levels either on the cell surface or in the serum increased in some neoplasms and decreased in others.

Expression system for standard: NS0; Immunogen sequence: S29-H760

cell culture supernatants, cell lysates, serum and plasma (heparin, EDTA).

Store at 4°C for 6 months, at -20°C for 12 months. Avoid multiple freeze-thaw cycles (Ships with gel ice, can store for up to 3 days in room temperature. Freeze upon receiving.)

Dipeptidyl peptidase 4

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..

Dipeptidyl peptidase 4