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P8234

Sigma-Aldrich

Anti-Serine/Threonine Protein Phosphatase 2 A/Bα antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.44

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 55 kDa

species reactivity

mouse, bovine, rat, human

concentration

~1 mg/mL

technique(s)

immunocytochemistry: 5-10 μg/mL
western blot: 5-10 μg/mL using total rat brain homogenate

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PPP2R2A(5520)

General description

Among the post-translational modifications, phosphorylation is a vital regulatory mechanism of key proteins involved in specific pathways. Reverse phosphorylation has become recognized as the key process of regulation of gene expression, cellular proliferation, differentiation in Eukaryotes. Protein phosphatases, like kinases, are a class of enzymes that regulate protein phosphorylation. The serine/threonine phosphatases have been classified into four groups which include PP1, PP2A, PP2B (also termed calcineurin) and PP2C on the basis of differences in their biochemical properties. Protein phosphatase 2A (PP2A) holozyme consists of a catalytic subunit (C), a structural subunit (A) and a regulatory subunit (B). The subunit B dictates the substrate specificity and is coded by at least 13 genes resulting in 3 distinct classes of subunits - α, β and γ. The B α subunit is targeted to the microtubules, renders substrate specificty and dephosphorylates cyclin-dependent kinase sites. The PP2A holoenzyme has been implicated in various functions such as cell cycle progression, oncogenic transformation and is subjected to tight regulation at the translational level, by post translational modifications and by protein-protein interations.
Anti-Serine/Threonine Protein Phosphatase 2A/Bα recognizes protein phosphatase 2A/Bα?isoforms of 55 kDa.

Immunogen

synthetic peptide (FSQVKGAVDDDVAE) corresponding to the N-terminus (amino acids 14-27) of the protein phosphatase 2A/Bα subunit.

Application

Anti-Serine/Threonine Protein Phosphatase 2A/B α may be used for detection at working concentration of 5-10 μg/mL in total rat brain homogenate. The antibody is also suitable for immunocytochemistry at a working concentration of 5-10 μg/mL.

Physical form

Provided as a 0.2 μm filtered solution in phosphate buffered saline containing 0.08% sodium azide.

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Storage Class

10 - Combustible liquids


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A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle
Sontag E et al
The Journal of Biological Chemistry, 128, 1131-1144 (1995)
A Cegielska et al.
Molecular and cellular biology, 14(7), 4616-4623 (1994-07-01)
The ability of simian virus 40 (SV40) large T antigen to catalyze the initiation of viral DNA replication is regulated by its phosphorylation state. Previous studies have identified the free catalytic subunit of protein phosphatase 2A (PP2Ac) as the cellular
R E Mayer-Jaekel et al.
Trends in cell biology, 4(8), 287-291 (1994-08-01)
Protein phosphorylation is probably the major regulatory mechanism employed by eukaryotic cells. Much work has been devoted to the role of protein kinases and their modulation by hormones, growth factors and neurotransmitters. It is now appreciated that protein phosphatases are
V Janssens et al.
The Biochemical journal, 353(Pt 3), 417-439 (2001-02-15)
Protein phosphatase 2A (PP2A) comprises a family of serine/threonine phosphatases, minimally containing a well conserved catalytic subunit, the activity of which is highly regulated. Regulation is accomplished mainly by members of a family of regulatory subunits, which determine the substrate
K Lechward et al.
Acta biochimica Polonica, 48(4), 921-933 (2002-05-09)
Protein phosphatase 2A (PP2A) comprises a diverse family of phosphoserine- and phosphothreonine-specific phosphatases present in all eukaryotic cells. All forms of PP2A contain a catalytic subunit (PP2Ac) which forms a stable complex with the structural subunit PR65/A. The heterodimer PP2Ac-PR65/A

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