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Key Documents

SAB1300598

Sigma-Aldrich

Anti-PPP2R1A (N-term) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-α isoform, Anti-PPP2R1A, Anti-Protein phosphatase 2 (Formerly 2A), Anti-Regulatory subunit A (PR 65)

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human

technique(s)

indirect ELISA: 1:1000
western blot: 1:100-1:500

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PPP2R1A(5518)

Related Categories

General description

PPP2R1A is a constant regulatory subunit of protein phosphatase 2. Protein phosphatase 2 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. The constant regulatory subunit A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit.

The previously assigned protein identifier Q96DH3 has beenmerged into P30153. Full details can be found on the UniProt database.

Immunogen

PPP2R1A (NP_055040, 90-124)
This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the N-terminal region of human PPP2R1A.

Physical form

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide.

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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Mingning Qiu et al.
Biochemical and biophysical research communications, 452(1), 163-169 (2014-08-26)
The aim of this study was to investigate the function of miR-183 in renal cancer cells and the mechanisms miR-183 regulates this process. In this study, level of miR-183 in clinical renal cancer specimens was detected by quantitative real-time PCR.
Toshiya Okumura et al.
PloS one, 9(6), e100559-e100559 (2014-06-20)
Phosphorylation of hormone-sensitive lipase (HSL) and perilipin by protein kinase A (PKA) promotes the hydrolysis of lipids in adipocytes. Although activation of lipolysis by PKA has been well studied, inactivation via protein phosphatases is poorly understood. Here, we investigated whether

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