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P1743

Sigma-Aldrich

Protein Phosphatase 2C from bovine brain

buffered aqueous glycerol solution

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CAS Number:
MDL number:
NACRES:
NA.32

biological source

bovine brain

Quality Level

Assay

>90% (SDS-GE)

form

buffered aqueous glycerol solution

specific activity

~1000 units/mg protein

mol wt

42-45 kDa

packaging

vial of 1 μg

technique(s)

ligand binding assay: suitable

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

bovine ... PPP2CA(282320)

General description

Protein phosphatase 2C (PP2C) is a member of protein phosphatases, Mg2+/Mn2+ dependent (PPM) family. PP2C is a monomeric enzymes found in both prokaryotes and eukaryotes.

Biochem/physiol Actions

In Arabidopsis, protein phosphatase 2C (PP2C) negatively regulates plant hormone, abscisic acid (ABA) signal transduction. In eukaryotes, this protein modulates the cell cycle by reversing the activating phosphorylation of cyclin-dependent protein kinases (CDKs). PP2C acts as a crucial physiological regulators of cell growth and of cellular stress signaling.

Unit Definition

One unit will release 1.0 nanomole of phosphate from 32P-labeled myelin basic protein 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

Signal Word

Warning

Hazard Statements

Hazard Classifications

Skin Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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ABI1 Protein Phosphatase 2C Is a Negative Regulator of Abscisic Acid Signaling
Gosti F, et al.
Plant Cell, 11, 1897-1910 (1999)
Plant PP2C phosphatases: emerging functions in stress signaling.
Schweighofer A, et al.
Trends in Plant Science, 9, 236-243 (2004)
Role of type 2C protein phosphatases in growth regulation and in cellular stress signaling.
Lammers T and Lavi S
Critical Reviews in Biochemistry and Molecular Biology, 42, 437-461 (2007)
A protein phosphatase 2C involved in ABA signal transduction in Arabidopsis thaliana
Meyer K, et al.
Science, 264, 1452-1455 (1994)

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