Protein Phosphatase, Lambda, Recombinant, E. coli

Recombinant λ PPase expressed in E. coli. A 221-amino acid, Mn²⁺-dependent, protein phosphatase. Hydrolyzes phosphate groups on serine, threonine, tyrosine, or histidine residues. Inhibited by orthovanadate. Note: 1KU = 1,000 units.

Research Area: Cell Signaling
The protein phosphatase encoded by bacteriophage λ (λPP) is part of a family of Ser/Thr phosphatases (Ser/Thr PPases), which includes eukaryotic protein phosphatases 1 (PP1), 2A (PP2A), and 2B (calcineurin).

Protein Phosphatase, Lambda, Recombinant, E. coli is suitable for the detection of phospho-KRAS.

Protein phosphatases play a crucial role in embryonic development, metabolic homeostasis, stress responses, cell cycle transitions, and numerous other vital biological processes.

Toxicity: Standard Handling (A)

One unit is defined as the amount of enzyme that will hydrolyze 1.0 nmol of pNPP per min at 30°C, pH 7.8. 20-200 Units will typically remove >95% of phosphates from serine/threonine residues in 0.1 nmol of protein in 30 min. 100-1000 Units will typically remove >95% of phosphates from tyrosine in 0.1 nmol of protein in 30 min.

In 100 mM NaCl, 50 mM HEPES, 2 mM DTT, 0.1 mM MnCl₂, 0.1 mM EGTA, 50% glycerol, 0.01% Brij^® 35 Detergent, pH 7.5.

Further dilute in 50 mM Tris-HCl, pH 7.8, 5 mM DTT, 2 mM MnCl₂, and 100 µg/ml BSA.

Following initial thaw, aliquot and freeze (-70°C).

Zhuo, S., et al. 1993. J. Biol. Chem.268, 17754.
Gordon, J.A. 1991. Methods Enzymol.201, 477.
Cohen, P.T.W. and Cohen, P. 1989. Biochem. J.260, 931.

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