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Merck

P1868

Sigma-Aldrich

Protein Phosphatase 2A2 from bovine kidney

buffered aqueous glycerol solution

Synonim(y):

PP2A2

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About This Item

Kod UNSPSC:
12352204
NACRES:
NA.54

pochodzenie biologiczne

bovine kidney

Poziom jakości

Postać

buffered aqueous glycerol solution

aktywność właściwa

~2.0 U/vial

masa cząsteczkowa

dimer 101 kDa (65 kDa and 36 kDa)

Warunki transportu

dry ice

temp. przechowywania

−70°C

Opis ogólny

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

Zastosowanie

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.

Działania biochem./fizjol.

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.

Definicja jednostki

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

Postać fizyczna

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.
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Piktogramy

Exclamation mark

Hasło ostrzegawcze

Warning

Zwroty wskazujące rodzaj zagrożenia

Zwroty wskazujące środki ostrożności

Klasyfikacja zagrożeń

Skin Sens. 1

Kod klasy składowania

10 - Combustible liquids

Klasa zagrożenia wodnego (WGK)

WGK 2

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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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