Protein Phosphatase 2C alpha, Recombinant, Human (PP2Ca, PPM1A, Protein Phosphatase, Mg2+/Mn2+ Dependent, 1A)

Protein phosphatase 2C alpha, also called PP2Calpha, Protein Phosphatase, Magnesium-dependent type 1A, and PPM1A, dephosphorylates proteins with some preference for phospho-threonine over phospho-serine residues 1. It is insensitive to the PP1 and PP2a inhibitors such as okadaic acid 2, but has an absolute requirement for either magnesium or manganese ions 3 and can be activated by unsaturated fatty acids such as arachidonic and oleic acids 4 . Overexpression of PP2Calpha causes G2/M cell cycle arrest and apoptosis that has been associated with the activation of p53 5 . Dephosphorylation of proteins in the nucleus by PP2Calpha is suspected to play a role in terminating or reducing the sensitivity of the responses to SMADS 6 and stress-activated proteins such as p38 and JNK 7.\n\nSource: E. coli-expressed recombinant protein.\n\nMolecular Mass: Amino acid residues 1-324 of PP2Calpha (Accession # NP_808820) with a C-terminal His6 sequence has a predicted molecular weight of 36.8kD.\n\nActivity: Measured by the ability to dephosphorylate Serine/Threonine Phosphatase Substrate II which has the amino acid sequence KRT(PO3)IRR. Assayed in a buffer containing 50 mM Tris, 10 mM MgCl2, 1 mg/mL BSA, 0.02% Brij-35, pH 7.5 for 30 minutes at 37 degrees C with shaking. 10 ng of enzyme cleaves 200 microM of phosphopeptide substrate with a specific activity of > 2 micromoles/min/mg.\n\nStorage and Stability: This product is shipped on dry ice. Upon receiving, aliquot immediately and store at -70 degrees C in a manual defrost freezer. Samples are stable for up to twelve months from the date of receipt. Avoid repeated freeze-thaw cycles.

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SPECIFICATIONS

Catalog Number

P9107-37B

Size

50ug

Form

Supplied as a liquid in 20mM HEPES, 50mM NaCl, 1mM MnCl2, 1mM DTT, pH 7.5.

Purity

(same/more than) 95%, as determined by SDS-PAGE and visualized by silver stain.

References

1. Donella-Deanna, A. et al. (1991) Biochimica et Biophysica Acta 1094:130. \n2. Bialojan, C. and A. Takai (1998) Biochem. J. 256:283. \n3. Cohen, P. Annu. Rev. Biochem. (1989) 58:453. \n4. Klumpp, S. et al. (1998) FEBS Let. 437:229. \n5. Ofek, P. et al. (2003) J. Biol. Chem. 278:14299. \n6. Lin, X. et al. (2006) Cell 125:915. \n7. Takekawa, M. et al. (1998) EMBO J. 17:4744.