P1743
Protein Phosphatase 2C from bovine brain
buffered aqueous glycerol solution
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About This Item
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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
Signal Word
Warning
Hazard Statements
Precautionary 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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ABI1 Protein Phosphatase 2C Is a Negative Regulator of Abscisic Acid Signaling
Gosti F, et al.
Plant Cell, 11, 1897-1910 (1999)
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)
Plant PP2C phosphatases: emerging functions in stress signaling.
Schweighofer A, et al.
Trends in Plant Science, 9, 236-243 (2004)
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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