PTPσ 抗体 (SS-8): sc-100419

PTPσ Antibody (SS-8) is an IgG_2b κ mouse monoclonal PTP sigma antibody (also designated PTPσ antibody) that detects the PTP sigma protein of human origin by WB, IP and ELISA. PTPσ Antibody (SS-8) is available as the non-conjugated anti-PTP sigma antibody. Protein tyrosine phosphatases, or PTPs, are type I transmembrane proteins, membrane associated proteins or proteins localized in nuclei. Examples of transmembrane PTPs are LAR, PTPα, PTPβ, PTPγ, PTPδ, PTPe, PTPΩ, PTPκ, PTPµ and PTPs. Transmembrane PTPs play diverse roles during development and in adult tissues. Immunodepletion studies have suggested LAR to be a regulator of insulin receptor phosphorylation. PTPα activity is increased twofold in response to phorbol ester stimulation, resulting in serine phosphorylation either directly or indirectly by members of the PKC family. Overexpression of v-H-Ras and Neu, but not Myc or Int2, in mammary tumors has been shown to induce PTPe expression. An alternative splicing event leads to a nervous tissue-specific chondroitin sulfate proteoglycan called phosphacan, which represents the amino terminal portion of PTPΩ. PTPκ and PTPµ share a conserved amino terminal 160 amino acid MAM domain which facilitates homophilic binding. PTPµ localizes to points of cell contact and may be involved in regulating the assembly and disassembly of cadherin/catenin complexes in vivo. PTPs contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. PTPs may also be involved in the molecular control of adult nerve repair. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported.

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References:

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2. Structural diversity and evolution of human receptor-like protein tyrosine phosphatases.  |  Krueger, NX., et al. 1990. EMBO J. 9: 3241-52. PMID: 2170109
3. The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions.  |  Serra-Pagès, C., et al. 1995. EMBO J. 14: 2827-38. PMID: 7796809
4. Molecular characterization of the human transmembrane protein-tyrosine phosphatase delta. Evidence for tissue-specific expression of alternative human transmembrane protein-tyrosine phosphatase delta isoforms.  |  Pulido, R., et al. 1995. J Biol Chem. 270: 6722-8. PMID: 7896816
5. Cloning and expression of two structurally distinct receptor-linked protein-tyrosine phosphatases generated by RNA processing from a single gene.  |  Pan, MG., et al. 1993. J Biol Chem. 268: 19284-91. PMID: 8396131
6. The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1.  |  Pulido, R., et al. 1995. Proc Natl Acad Sci U S A. 92: 11686-90. PMID: 8524829
7. Protein tyrosine phosphatases in signal transduction.  |  Neel, BG. and Tonks, NK. 1997. Curr Opin Cell Biol. 9: 193-204. PMID: 9069265
8. The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma.  |  Wallace, MJ., et al. 1998. Mol Cell Biol. 18: 2608-16. PMID: 9566880