Anti-Mouse CD318 In Vivo Antibody – Low Endotoxin (9a2) [ICH1165]

CDCP1 is a transmembrane glycoprotein of molecular weight 140 kDa. CDCP1 is a ligand for a receptor molecule (CD6) that is expressed on some T-cells and is thought to be involved in T-cell migration and chemotaxis. It has a large extracellular domain that includes two CUB domains, and a smaller intracellular domain. The smaller intracellular domain contains five tyrosine residues (Y707, Y734, Y743, Y762 and Y806). CDCP1 is cleaved next to Arg368 (at the extracellular domain) by serine proteases. This cleavage yields a truncated molecule with a molecular weight of 80 kDa.1 CDCP1 is not typically cleaved In vivo. However, its cleavage can be induced during tumorigenesis or tissue injury.2 CDCP1 acts as a substrate for Src family kinases which exclusively mediate the phosphorylation of CDCP1. In cultured cells, tyrosine phosphorylation of CDCP1 transpires when cells are stimulated to detach via trypsin or EDTA. This detachment is associated with the phosphorylation of CDCP1 along with the simultaneous dephosphorylation of focal adhesion proteins. Conversely, during cellular attachment, CDCP1 is dephosphorylated, while focal adhesion proteins are simultaneously phosphorylated. Furthermore, CDCP1 is suspected to play a role in autoimmune diseases such as encephalomyelitis, multiple sclerosis and inflammatory arthritis.3