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DEP1 Antibody (C-term) Blocking Peptide
Synthetic peptide
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- BACKGROUND
| Primary Accession | Q12913 |
|---|---|
| Clone Names | 2011607 |
| Gene ID | 5795 |
|---|---|
| Other Names | Receptor-type tyrosine-protein phosphatase eta, Protein-tyrosine phosphatase eta, R-PTP-eta, Density-enhanced phosphatase 1, DEP-1, HPTP eta, Protein-tyrosine phosphatase receptor type J, R-PTP-J, CD148, PTPRJ, DEP1 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP8402a was selected from the C-term region of human DEP1 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | PTPRJ |
|---|---|
| Synonyms | DEP1 |
| Function | Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2 (PubMed:10821867, PubMed:12062403, PubMed:12370829, PubMed:12475979, PubMed:18348712, PubMed:19494114, PubMed:19922411, PubMed:21262971). Plays a role in cell adhesion, migration, proliferation and differentiation (PubMed:12370829, PubMed:14709717, PubMed:16682945, PubMed:19836242). Involved in vascular development (By similarity). Regulator of macrophage adhesion and spreading (By similarity). Positively affects cell-matrix adhesion (By similarity). Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation (PubMed:16682945). Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR (PubMed:21091576). Positive regulator of endothelial cell survival, as well as of VEGF- induced SRC and AKT activation; through KDR dephosphorylation (PubMed:18936167). Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation (PubMed:19836242). Enhances the barrier function of epithelial junctions during reassembly (PubMed:19332538). Negatively regulates T-cell receptor (TCR) signaling (PubMed:9531590, PubMed:9780142, PubMed:11259588). Upon T-cell TCR activation, it is up- regulated and excluded from the immunological synapses, while upon T- cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling (PubMed:11259588, PubMed:12913111). |
| Cellular Location | Cell membrane; Single-pass type I membrane protein. Cell projection, ruffle membrane. Cell junction Note=After T-cell stimulation, it is temporarily excluded from immunological synapses |
| Tissue Location | Expressed in the promyelocytic cell line HL-60, the granulocyte-macrophage colony-stimulating factor-dependent leukemic cell line F-36P, and the IL3 and erythropoietin-dependent leukemic cell line F-36E. Expressed predominantly in epithelial cells and lymphocytes. Enhanced expression at high cell density |
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Provided below are standard protocols that you may find useful for product applications.
Background
DEP1 is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region containing five fibronectin type III repeats, a single transmembrane region, and a single intracytoplasmic catalytic domain, and thus represents a receptor-type PTP. This PTP is present in all hematopoietic lineages, and was shown to negatively regulate T cell receptor signaling possibly through interfering with the phosphorylation of Phospholipase C Gamma 1 (PLCG1) and Linker for Activation of T Cells (LAT). This PTP was also found to dephosphorylate PDGF beta receptor, and may be involved in UV-induced signal transduction.
References
Dong, H.Y., et al., Leuk. Lymphoma 43(9):1855-1858 (2002).Ruivenkamp, C.A., et al., Nat. Genet. 31(3):295-300 (2002).Baker, J.E., et al., Mol. Cell. Biol. 21(7):2393-2403 (2001).Kovalenko, M., et al., J. Biol. Chem. 275(21):16219-16226 (2000).Gross, S., et al., J. Biol. Chem. 274(37):26378-26386 (1999).
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