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Key Documents

P1868

Sigma-Aldrich

Protein Phosphatase 2A2 from bovine kidney

buffered aqueous glycerol solution

Synonym(s):

PP2A2

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine kidney

Quality Level

form

buffered aqueous glycerol solution

specific activity

~2.0 U/vial

mol wt

dimer 101 kDa (65 kDa and 36 kDa)

shipped in

dry ice

storage temp.

−70°C

General description

Protein phosphatase 2A (PP2A) is a specific protamine-kinase-inactivating phosphatase, one common physiological form of which is PP2A2.

Application

Protein phosphatase 2A2 has been used in a study to investigate two heat-stable protein inhibitors. It has also been used in a study to describe the purification and properties of a protamine kinase from bovine kidney microsomes.

Biochem/physiol Actions

Protein Phosphatase 2A2 from bovine kidney was shown to be a unique inhibitor of protamine kinase while other phosphatases in the same family including PP1, PP2B, PP2C did not show any inhibition.

Unit Definition

One unit will release 1 nanomole of inorganic phosphate from (32)P-labeled phosphorylase per minute at pH 7.0 at 30 deg C.

Physical form

Solution of 1 μg per vial in 50 μl of 50 mM Tris-HCl, pH 7.0, containing 14 mM β-Mercaptoethanol, 1mM benzamidine, 0.1 mM PMSF, 1mM EDTA, and 50% glycerol.

Pictograms

Exclamation mark

Signal Word

Warning

Hazard Statements

Hazard Classifications

Skin Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Protein Phosphatase 2A is a specific protamine-kinase-inactivating phosphatase.
Amick, G.D, et al.
The Biochemical Journal, (Pt 3), 1019-1022 (1992)
G D Amick et al.
Archives of biochemistry and biophysics, 297(1), 80-85 (1992-08-15)
About an eightfold increase in protamine kinase activity was detected following extraction of highly purified microsomes from bovine kidney with 1% Triton X-100. Relative to the soluble fraction, the microsomes contained about 30% protamine kinase activity. The microsomal protamine kinase
H R Matthews et al.
FEBS letters, 364(1), 51-54 (1995-05-01)
Whole cell extracts from rat liver or spinach leaves contain divalent ion-independent protein histidine phosphatase activity due to phosphatases of the PP1/PP2A family. In the rat liver extract, almost all the activity was found in the PP1, PP2A1 and PP2A2
M Li et al.
Biochemistry, 34(6), 1988-1996 (1995-02-14)
Two heat-stable protein inhibitors of protein phosphatase 2A (PP2A), tentatively designated I1PP2A and I2PP2A, have been purified to apparent homogeneity from extracts of bovine kidney. The purified preparations of I1PP2A exhibited an apparent M(r) approximately 30,000 and 250,000 as determined
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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