Human DEP‑1/CD148 Fluorescein‑conjugated Antibody

Density Enhanced Protein Tyrosine Phosphatase (DEP-1), also known as CD148, HPTP-eta, and PTP Receptor Type J (PTPRJ), is an enzyme that removes phosphate groups covalently attached to tyrosine residues in proteins. A large (220 kDa) glycoprotein found at the cell surface, DEP-1 levels are increased with high cell density (1). DEP-1 phosphatase activity is enhanced by basement membrane proteins (2), suggesting it is involved in regulating cell adhesion and contact interactions. High levels of expression dampen PDGF (3), VEGF (4), and T-cell receptor (5) responses. DEP-1 is widely expressed in tissues, particularly ones forming epithelioid monolayers (6). In the immune system, DEP-1 is found on all cell lineages and is highest on granulocytes (7). Dep-1 is the mutated gene in the Susceptibility to Colon Cancer locus Scc1, which is altered in many human colorectal adenomas (8). Gene knockout mice lacking DEP-1 die at midgestation due to failures in cardiovascular development (9). DEP-1 dephosphorylates a variety of proteins, including the HGF (10), PDGF (11), and VEGF (4) receptors, and beta-Catenin (12). The recombinant protein is the intracellular region of DEP-1 containing the catalytic domain.