|Application ||WB, E|
|Calculated MW||90600 Da|
|Antigen Region||89-120 aa|
|Other Names||Receptor-type tyrosine-protein phosphatase alpha, Protein-tyrosine phosphatase alpha, R-PTP-alpha, PTPRA, PTPA, PTPRL2|
|Target/Specificity||This PTP alpha antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 89-120 amino acids from the N-terminal region of human PTP alpha.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PTP alpha Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Cellular Location||Membrane; Single-pass type I membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
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.
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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