PPP2R5B Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
|Application ||WB, IF, E|
|Calculated MW||57393 Da|
|Other Names||Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform, PP2A B subunit isoform B'-beta, PP2A B subunit isoform B56-beta, PP2A B subunit isoform PR61-beta, PP2A B subunit isoform R5-beta, PPP2R5B|
|Target/Specificity||This PPP2R5B antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 466-500 amino acids from the C-terminal region of human PPP2R5B.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|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||PPP2R5B Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||As the regulatory component of the serine/threonine- protein phosphatase 2A (PP2A) holoenzyme, modulates substrate specificity, subcellular localization, and responsiveness to phosphorylation. The phosphorylated form mediates the interaction between PP2A and AKT1, leading to AKT1 dephosphorylation.|
|Tissue Location||Highest expression in brain.|
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Provided below are standard protocols that you may find useful for product applications.
The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The phosphorylated form mediates the interaction between AKT1 and PP2A phosphatase leading to dephosphorylation of AKT1 on the 'Thr-308' and 'Ser-373' residues.
McCright B.,et al.J. Biol. Chem. 270:26123-26128(1995).
Zolnierowicz S.,et al.Biochem. J. 317:187-194(1996).
McCright B.,et al.J. Biol. Chem. 271:22081-22089(1996).
Kitajima T.S.,et al.Nature 441:46-52(2006).
Rodgers J.T.,et al.Mol. Cell 41:471-479(2011).
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