|Other Names||Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform, PP2A-alpha, Replication protein C, RP-C, PPP2CA|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP8462b was selected from the C-term region of human PPP2CA/B. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|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.|
|Function||PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGOL2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at 'Ser-259'.|
|Cellular Location||Cytoplasm. Nucleus. Chromosome, centromere. Cytoplasm, cytoskeleton, spindle pole. Note=In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles. Centromeric localization requires the presence of SGOL2 (By similarity).|
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Provided below are standard protocols that you may find useful for product applications.
PPP2CA/B represents the phosphatase 2A catalytic subunit. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits.
Gergs, U., et al., J. Biol. Chem. 279(39):40827-40834 (2004).Prickett, T.D., et al., J. Biol. Chem. 279(37):38912-38920 (2004).Scott, G.K., et al., EMBO J. 22(23):6234-6244 (2003).Rao, R.K., et al., Biochem. Biophys. Res. Commun. 293(1):610-616 (2002).Avdi, N.J., et al., J. Biol. Chem. 277(43):40687-40696 (2002).
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