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.[1]
Biochem/physiol Actions
In Arabidopsis, protein phosphatase 2C (PP2C) negatively regulates plant hormone, abscisic acid (ABA) signal transduction.[2][3] In eukaryotes, this protein modulates the cell cycle by reversing the activating phosphorylation of cyclin-dependent protein kinases (CDKs).[1] PP2C acts as a crucial physiological regulators of cell growth and of cellular stress signaling.[4]
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
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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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