PTP mu Antibody (N-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P28827 |
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Clone Names | 1121702 |
Gene ID | 5797 |
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Other Names | Receptor-type tyrosine-protein phosphatase mu, Protein-tyrosine phosphatase mu, R-PTP-mu, PTPRM, PTPRL1 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP8419a was selected from the N-term region of human PTPmu . 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 | PTPRM |
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Synonyms | PTPRL1 |
Function | Receptor protein-tyrosine phosphatase that mediates homotypic cell-cell interactions and plays a role in adipogenic differentiation via modulation of p120 catenin/CTNND1 phosphorylation (PubMed:17761881, PubMed:10753936). Promotes CTNND1 dephosphorylation and prevents its cytoplasmic localization where it inhibits SLC2A4 membrane trafficking. In turn, SLC2A4 is directed to the plasma membrane and performs its glucose transporter function (PubMed:21998202). |
Cellular Location | Cell membrane; Single-pass type I membrane protein. Note=Localizes in regions of cell- cell contact. |
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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
Hoffmann, K.M., et al., J. Biol. Chem. 272(44):27505-27508 (1997).Gebbink, M.F., et al., FEBS Lett. 290 (1-2), 123-130 (1991).
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