DEP-1 Antibody (D-4): sc-376792

DEP-1 Antibody (D-4) is a mouse monoclonal IgG2b antibody that detects density-enhanced phosphatase-1 (DEP-1) in human samples through various applications including western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry with paraffin-embedded sections (IHCP), and enzyme-linked immunosorbent assay (ELISA). DEP-1, also known as HPTP-eta/CD148, plays a crucial role in signal transduction within leukocytes and is integral to cellular differentiation processes. DEP-1 features a unique structure comprising an extracellular segment with eight fibronectin type III repeats, a single transmembrane segment, and an intracellular protein tyrosine phosphatase domain, which collectively facilitate function in modulating cellular signaling pathways. DEP-1 is widely expressed in lymphoid organs, particularly on B and T cells, granulocytes, macrophages, and certain dendritic cells, as well as in non-lymphoid tissues such as fibrocytes and melanocytes. DEP-1′s ability to inhibit T cell receptor-mediated activation in Jurkat T cells underscores importance in regulating immune responses, leading to decreased expression of early activation markers and inhibiting phosphorylation of key intracellular proteins, including tyrosine kinase ZAP-70. Despite intrinsic enzymatic activity, DEP-1 can paradoxically induce protein tyrosine phosphorylation in human lymphocytes and modulate serine/threonine and tyrosine phosphorylation in various tumor cell lines, highlighting complex role in cellular signaling and potential implications in cancer biology.

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DEP-1 Antibody (D-4) References:

1. The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation.  |  Kellie, S., et al. 2004. J Cell Sci. 117: 609-18. PMID: 14709717
2. DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients.  |  Balavenkatraman, KK., et al. 2006. Oncogene. 25: 6319-24. PMID: 16682945
3. An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis.  |  Tarcic, G., et al. 2009. Curr Biol. 19: 1788-98. PMID: 19836242
4. Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling.  |  Arora, D., et al. 2011. J Biol Chem. 286: 10918-29. PMID: 21262971
5. Cell transformation by FLT3 ITD in acute myeloid leukemia involves oxidative inactivation of the tumor suppressor protein-tyrosine phosphatase DEP-1/ PTPRJ.  |  Godfrey, R., et al. 2012. Blood. 119: 4499-511. PMID: 22438257
6. Tyrosine phosphorylation of DEP-1/CD148 as a mechanism controlling Src kinase activation, endothelial cell permeability, invasion, and capillary formation.  |  Spring, K., et al. 2012. Blood. 120: 2745-56. PMID: 22898603
7. Phosphorylation of DEP-1/PTPRJ on threonine 1318 regulates Src activation and endothelial cell permeability induced by vascular endothelial growth factor.  |  Spring, K., et al. 2014. Cell Signal. 26: 1283-93. PMID: 24583284
8. Deficiency of the protein-tyrosine phosphatase DEP-1/PTPRJ promotes matrix metalloproteinase-9 expression in meningioma cells.  |  Petermann, A., et al. 2015. J Neurooncol. 122: 451-9. PMID: 25672645
9. Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density.  |  Ostman, A., et al. 1994. Proc Natl Acad Sci U S A. 91: 9680-4. PMID: 7937872
10. The receptor-like protein-tyrosine phosphatase DEP-1 is constitutively associated with a 64-kDa protein serine/threonine kinase.  |  Jallal, B., et al. 1997. J Biol Chem. 272: 12158-63. PMID: 9115287

The preferred DEP-1 antibody is DEP-1 Antibody (143-41): sc-21761.