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Merck

P5359

Sigma-Aldrich

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

~1 mg/mL, IgG fraction of antiserum, 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

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 56 kDa

species reactivity

human, rat, bovine, mouse

concentration

~1 mg/mL

technique(s)

microarray: suitable
western blot: 1:10 μg/mL using total rat brain homogenate

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... PPP2R2C(5522)

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 γ subunit is targeted to the nucleus. 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/B γ specifically recognizes 56 kDa protein phosphatase 2A/B γ isoforms.

Immunogen

synthetic peptide (REPSKNAPHSQGE) corresponding to the internal conserved sequence (amino acids 53-66) of mammalian protein phosphatase 2 A/B γ.

Application

The recommended concentration for detection by immunoblotting is 1-10 μg/mL using peroxidase conjugated goat anti-rabbit IgG and chemiluminescent detection.

Physical form

Solution in phosphate buffered saline, pH 7.2-7.4, containing 0.08% sodium azide.

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Storage Class

10 - Combustible liquids


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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
Serine/threonine protein phosphatases.
S Wera et al.
The Biochemical journal, 311 ( Pt 1), 17-29 (1995-10-01)
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
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

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