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SAB4200266

Sigma-Aldrich

Anti-PP2A, C subunit antibody, Mouse monoclonal

clone 7A6, purified from hybridoma cell culture

Synonym(s):

MonoclonalAnti-PP2Ac, MonoclonalAnti-PP2CA, MonoclonalAnti-PP2Calpha, MonoclonalAnti-PPP2CA, MonoclonalAnti-RP-C, MonoclonalAnti-protein phosphatase 2, catalytic subunit, alpha isozyme

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.44

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

7A6, monoclonal

form

buffered aqueous solution

mol wt

antigen 36 kDa

species reactivity

human, mouse, rat

concentration

~1.0 mg/mL

technique(s)

immunoprecipitation (IP): suitable
western blot: 1-2 μg/mL using whole extracts of mouse 3T3, rat Rat2 or human A431 cells.

isotype

IgG1

UniProt accession no.

P67775

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PPP2CA(5515)
mouse ... Ppp2ca(19052)
rat ... Ppp2ca(24672)

Related Categories

General description

PP2A is a serine/threonine phosphatase that downregulates the MAP kinase pathway and subsequently modulates mitogenic signaling. This phosphatase also mediates localization of Sgo1 at centromeres, Ras-1 activation, and chromosome segregation. The catalytic subunit of PP2A (PP2Ac) regulates the signaling pathway for glucose-stiμLated insulin secretion .

Specificity

Monoclonal Anti-PP2Ac is specific for the α and β isoforms of PP2Ac in humans, rats and mice. The antibody has not been tested in other species for cross-reactivity.

Application

MonoclonalAnti-PP2A, C subunit antibody produced in mouse has been used in immunoblotting and immunoprecipitation.

Biochem/physiol Actions

Protein phosphatase 2A (PP2A) is implicated in the negative control of cell growth and division. PP2Ac undergoes two post-translational modifications, phosphorylation and methylation, which are involved in the regulation of the enzyme activity.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Donghai Liu et al.
Nature communications, 12(1), 2551-2551 (2021-05-07)
Endogenous cardiac pacemaker function regulates the rate and rhythm of cardiac contraction. The mutation p.Lys23Glu in the cohesin protein Shugoshin-1 causes severe heart arrhythmias due to sinoatrial node dysfunction and a debilitating gastrointestinal motility disorder, collectively termed the Chronic Atrial
PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.
Hegarat N, Vesely C, Vinod PK, et al.
PLoS Genetics, 10(1), e1004004-e1004004 (2014)
Giridhar R Jangati et al.
Endocrine, 31(3), 248-253 (2007-10-02)
Among various phosphatases, the protein phosphatase 2A (PP2A) is relatively well studied in the islet. Previously, we have demonstrated that the catalytic subunit of PP2A (PP2Ac) undergoes okadaic acid (OKA)-sensitive, reversible carboxylmethylation (CML), which appears to be requisite for glucose-stimulated
Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
Janssens V and Goris J
The Biochemical Journal, 353(3), 417-439 (2001)
Nadia Hégarat et al.
PLoS genetics, 10(1), e1004004-e1004004 (2014-01-07)
Entry into mitosis is triggered by activation of Cdk1 and inactivation of its counteracting phosphatase PP2A/B55. Greatwall kinase inactivates PP2A/B55 via its substrates Ensa and ARPP19. Both Greatwall and Ensa/ARPP19 are regulated by phosphorylation, but the dynamic regulation of Greatwall
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