Human/Mouse/Rat DEP-1/CD148 Alexa Fluor® 647-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: DEP-1/CD148

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 kilodalton) 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. Over aa 997-337, human Dep-1 shares 95% aa sequence identity with mouse  and rat Dep-1.

Product Datasheets

Related Research Areas

• Adhesion Molecules on Endothelial Cells
• B Cell Markers
• Epigenetics
• Granulocyte Markers
• Monocyte Markers
• Phosphatases and Regulators
• Phosphatases in the Akt Pathway
• Platelet Immune Receptors
• Search Kinases and Phosphatases