|Other Accession||P23696, P63331, P67777, P67776, P63330, P67774, NP_002706.1|
|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 is selected from aa 103-116 of HUMAN PPP2CA|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI 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 SGO2 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 SGO2 (By similarity).|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes 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. This gene encodes an alpha isoform of the catalytic subunit.
Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)
Jayadeva, G., et al. J. Biol. Chem. 285(39):29863-29873(2010)
Pradhan, S., et al. J. Biol. Chem. 285(38):29059-29068(2010)
Schmitz, M.H., et al. Nat. Cell Biol. 12(9):886-893(2010)
Antony, R., et al. J. Biol. Chem. 285(24):18301-18308(2010)
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