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P6993

Sigma-Aldrich

Protein Phosphatase 2A1 bovine

≥1500 units/mg protein

Sinónimos:

PPA2A1

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About This Item

MDL number:
MFCD00241719
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine

Quality Level

200

assay

≥90% (SDS-PAGE)

form

solution

specific activity

≥1500 units/mg protein

mol wt

192 kDa

packaging

vial of 1 μg

shipped in

dry ice

storage temp.

−70°C

General description

Protein Phosphatase 2A1 (PP2A1) belongs to the PP2A family and comprises trimeric A, B and C subunits. PPA2 enzymes are serine/threonine phosphatases and exist as several isoforms.

Application

Protein phosphatase 2A1 has been used to treat human fibroblast cells prior to western blot analysis.

Biochem/physiol Actions

Protein Phosphatase 2A is a cytoplasmic protein, which colocalizes with microtubule proteins and is involved in the dephosphorylation of the tau protein and oncoprotein 18. Protein Phosphatase 2A1 (PP2A1) binds to polymerized microtubule proteins and may be targeted by tubulin in modulating phosphatase activity. PP2A1 is implicated as a growth suppressor and is associated with dysregulation in cancer. It also regulates cell cycle, RNA splicing differentiation, and signal transduction. PP2A dysfunction is correlated to the tau protein deregulation in Alzheimer′s disease pathophysiology. Protein Phosphatase 2A1 is a divalent cation-dependent protein serine/threonine phosphatase implicated as a growth suppressor and is associated with dysregulation in cancer.

Unit Definition

One unit will release 1.0 nanomole of phosphate from 32P-labeled phosphorylase A per minute at pH 7.0 at 30 °C.

Physical form

Solution in 50 mM Tris-HCl, pH 7.0, containing 14 mM 2-mercaptoethanol, 1 mM benzamidine, 0.1 mM PMSF, 1 mM EDTA, and 50% glycerol

pictograms

Exclamation mark
GHS07

signalword

Warning

hcodes

H317

Hazard Classifications

Skin Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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K Webley et al.
Molecular and cellular biology, 20(8), 2803-2808 (2000-03-25)
Replicative senescence in human fibroblasts is absolutely dependent on the function of the phosphoprotein p53 and correlates with activation of p53-dependent transcription. However, no evidence for posttranslational modification of p53 in senescence has been presented, raising the possibility that changes
A Hiraga et al.
The Biochemical journal, 346 Pt 2, 433-439 (2000-03-24)
Protein phosphatase (PP) 2A1, a trimer composed of A-, B- and C-subunits in the PP2A family, has been regarded as a principal form localizing at microtubules (MT), but PP2A2, the dimer of A- and C-subunits, has not. Substantiating the claim

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