PTPRA is a transmembrane phosphatase that regulates cell proliferation, cell adhesion, integrin signaling, and growth factor response. This phosphatase also activates proteins of the Src family. PTPRA inhibits cell growth in breast cancer and contributes to tumorigenesis in colon carcinoma . Anti-PTPRA antibody is specific for human and mouse PTPRA. In immunoblotting, detection of the PTPRA band is specifically inhibited by the immunizing peptide.
Protein tyrosine phosphatase alpha (PTPRA) is a transmembrane phosphatase with a relatively short, highly glycosylated extracellular domain, a transmembrane domain, and a tandem phosphatase domain. The amino-terminal domain predominantly mediates catalytic activity, whereas the carboxyterminal domain serves as a regulatory subunit.
Immunogen
synthetic peptide corresponding to an internal region of human PTPRA, conjugated to KLH. The corresponding sequence is identical in mouse and differs by one amino acid in rat.
Application
Anti-PTPRA antibody is suitable for use in western blot (0.25-0.5 μg/mL using lysates of NIH-3T3 or PC12 cells) and indirect immunofluorescence (5-10 μg/mL using paraformaldehyde fixed HUVEC cells).
Anti-PTPRA antibody produced in rabbit has been used in immunoblotting and immunofluorescence.
Biochem/physiol Actions
Protein tyrosine phosphatase alpha (PTPRA) is implicated in several signaling pathways, including insulin receptor signaling, cellular transformation and cell spreading and migration. It regulates cell proliferation, cell adhesion, integrin signaling, and growth factor response. PTPRA inhibits cell growth in breast cancer and contributes to tumorigenesis in colon carcinoma.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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The protein tyrosine phosphatase alpha (PTP alpha) mRNA level in paired samples of late stage (Dukes' D) colorectal tumors and adjacent normal colon mucosa was quantified by RNase protection assays. After normalization against 18S RNA or beta-actin mRNA level, a
Protein tyrosine phosphatases (PTPases), together with protein tyrosine kinases, regulate the tyrosine phosphorylation that controls cell activities and proliferation. Previously, it has been recognized that both cytosolic PTPases and membrane associated, receptor-like PTPases exist. In order to examine the structural
Tyrosine phosphorylation is controlled by a balance of tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). Whereas the contribution of PTKs to breast tumorigenesis is the subject of intense scrutiny, the potential role of PTPs is poorly known. RPTPalpha is
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