CD26/Dipeptidyl Peptidase 4 Protein, Human (HEK293)

CD26/Dipeptidyl Peptidase 4 protein, a cell surface glycoprotein receptor, plays a pivotal role in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Functioning as a positive regulator of T-cell coactivation, CD26 interacts with ADA, CAV1, IGF2R, and PTPRC, leading to T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its binding to CAV1 and CARD11 induces T-cell proliferation, while its interaction with ADA regulates lymphocyte-epithelial cell adhesion. In association with FAP, CD26 is involved in pericellular proteolysis of the extracellular matrix, contributing to the migration and invasion of endothelial cells. Additionally, it may play a role in promoting lymphatic endothelial cell adhesion, migration, and tube formation. Acting as a serine exopeptidase with dipeptidyl peptidase activity, CD26 regulates various physiological processes by cleaving peptides in the circulation, including chemokines, mitogenic growth factors, neuropeptides, and peptide hormones. Notably, CD26 acts as a receptor for the human coronavirus MERS-CoV-2 during microbial infection. CD26/Dipeptidyl Peptidase 4 Protein, Human (HEK293) is the recombinant human-derived CD26/Dipeptidyl Peptidase 4 protein, expressed by HEK293 , with tag free. The total length of CD26/Dipeptidyl Peptidase 4 Protein, Human (HEK293) is 738 a.a., with molecular weight of ~95 kDa.

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Recombinant Proteins