PTP alpha Antibody (N-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P18433 |
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Clone Names | 1123008 |
Gene ID | 5786 |
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Other Names | Receptor-type tyrosine-protein phosphatase alpha, Protein-tyrosine phosphatase alpha, R-PTP-alpha, PTPRA, PTPA, PTPRL2 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP8412a was selected from the N-term region of human PTPalpha . 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 | PTPRA |
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Synonyms | PTPA, PTPRL2 |
Function | Tyrosine protein phosphatase which is involved in integrin- mediated focal adhesion formation (By similarity). Following integrin engagement, specifically recruits BCAR3, BCAR1 and CRK to focal adhesions thereby promoting SRC-mediated phosphorylation of BRAC1 and the subsequent activation of PAK and small GTPase RAC1 and CDC42 (By similarity). |
Cellular Location | Cell membrane; Single-pass type I membrane protein. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P18052}. Note=Localizes to focal adhesion sites following integrin engagement. {ECO:0000250|UniProtKB:P18052} |
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Provided below are standard protocols that you may find useful for product applications.
Background
Phosphorylation of receptors by protein kinases is a process that can be reversed by a group of enzymes called protein phosphatases. Coordinated control of kinases and phosphatases provides the cell with the capacity to rapidly switch between phosphorylated and dephosphorylated protein states in dynamic response to environmental stimuli. Activation of critical enzymes by kinase phosphorylation alone is not enough to provide adequate regulation ? it is the combination with phosphatase dephosphorylation that effectively creates on/off switches to control cellular events. Errors in control, either through kinases or their counterpart phosphatases, can lead to unchecked cell growth attributable to human cancers and developmental disorders. Potential mechanisms to control dephosphorylation include changes in the expression of protein phosphatases, their subcellular localization, phosphorylation of phosphatase catalytic and regulatory subunits and regulation by endogenous phosphatase inhibitors. Most protein phosphatases are not stringently specific for their substrates. Consequently, changes in phosphatase activity may have a broad impact on dephosphorylation and turnover of phosphoproteins that are substrates for different kinases. This may be an important point of control to connect cellular circuitry of interrelated signaling pathways, and to synchronize physiological responses.
References
Deloukas, P., et al., Nature 414(6866):865-871 (2001).Kaplan, R., et al., Proc. Natl. Acad. Sci. U.S.A. 87(18):7000-7004 (1990).Krueger, N.X., et al., EMBO J. 9(10):3241-3252 (1990).Sap, J., et al., Proc. Natl. Acad. Sci. U.S.A. 87(16):6112-6116 (1990).Jirik, F.R., et al., FEBS Lett. 273 (1-2), 239-242 (1990).
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