Anti-PTPζ Antibody (122.2): sc-33664

PTPζ Antibody (122.2) is a high quality monoclonal PTP zeta antibody (also designated PTPRZ antibody, Protein Tyrosine Phosphatase Receptor Type Z1 antibody, Receptor-Type Tyrosine-Protein Phosphatase Zeta antibody, R-PTP-Zeta-2 antibody, Phosphacan antibody, PTP18 antibody, PTPRZ antibody, RPTPB antibody, PTPZ antibody, Protein Tyrosine Phosphatase Receptor-Type Zeta antibody, Receptor-Type Tyrosine Phosphatase Beta/Zeta antibody, R-PTP-Zeta antibody, HPTPzeta antibody, PTP-ZETA antibody, RPTPbeta antibody, HTPZP2 antibody, PTPRZ2 or HPTPZ antibody) suitable for the detection of the PTP zeta protein of mouse, rat and human origin. PTPζ Antibody (122.2) is available as the non-conjugated anti-PTP zeta 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, PTPζ, PTPκ and PTPµ. 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 PTPζ. 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.