Background:  Protein tyrosine phosphatases, or PTPs, are type I transmembrane proteins, membrane associated proteins or proteins localized in nuclei. Examples of transmembrane PTPs are LAR, PTP α, PTP β, PTP γ, PTP δ, PTP ε, PTP ζ, PTP κ and PTP μ. Transmembrane PTPs play diverse roles during development and in adult tissues. Immunodepletion studies have suggested LAR to be a regu-lator of insulin receptor phosphorylation. PTP αactivity 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 PTP ε expression. PTP μ localizes to points of cell contact and may be involved in regulating the assembly and disassembly of cadherin/catenin complexes in vivo . PTP μ and PTP κ share a conserved amino-terminal 160 amino acid MAM domain which facilitates homophilic binding. An alternative splicing event leads to a nervous tissue-specific chondroitin sulfate proteo-glycan called phosphacan, which represents the amino-terminal portion of PTPζ.

Description: Rabbit polyclonal to PTPRF

Immunogen: KLH conjugated synthetic peptide derived from PTPRF

Specificity:  ·Reacts with Human, Mouse and Rat.

·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 210 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;

·Immunocytochemistry/Immunofluorescence: 1/100;

·Immunoprecipitation: 1/50;

·ELISA: 1/500;

·Optimal working dilutions must be determined by the end user.