Biochemical Reagents for Enzymes and proteins

Lambda Protein Phosphatase


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Background

λ Protein Phosphatase (λ -PPase) is a Mn+2-dependent protein phosphatase with activity towards phosphorylated serine, threonine, tyrosine and histidine residues. It is the 221 amino-acid product of ORF221 open reading frame on bacteriophage lambda (1,2). λ -PPase was expressed as a recombinant protein in E.coli and highly purified (2). This product is an intact enzyme of high quality without tag.

Data Link  Swiss-Prot P03772

< Reference >
1. Cohen,P.T.W., Cohen, P. (1989) “Discovery of a protein phosphatase activity encoded in the genome of bacteriophage λ.” Biochem J. 260: 931-934 PMID: 2548489
2. Zhuo,S. et al. (1993) “Expression, purification, crystallization, and biochemical characterization of recombinant protein phosphatase.” J. Biol. Chem. 268: 17754-17761 PMID: 8394350

Application

λ -PPase can be used to release phosphate groups from phosphorylated serine, threonine, tyrosine and histidine residues in proteins (2). It should be noted that different proteins are dephosphorylated at different rates. Optimal reaction temperature is 30 degrees. Inclusion of protease inhibitor cocktail and shortest incubation time is desired when assays are done with crude samples.

< Activity>
400 U/μl, where one unit is defined as the amount of enzyme that hydrolyzes 1 nmole of p-nitrophenyl phosphate per minute at 30 degrees. Unit definition assays are performed with 50mM p-nitrophenyl phosphate in λ -PPase buffer, supplemented with 2 mM MnCl2 in a 50 μl reaction.

< Specific Activity >
400,000 U / mg

< SDS-PAGE of λ-PPase >
Greater than 95% homogeneous protein determined by SDS-PAGE (CBB staining) that contains no detectable protease activity.

Product List

Product Name Cat# Quantity Price

Lambda Protein Phosphatase DataSheet ,

BAM-02-300-EX

20000 UNIT ¥11,000
$147

Lambda Protein Phosphatase DataSheet ,

BAM-02-300-5EX

5*20000 UNIT ¥44,000
$587

To be used for research only. DO NOT use for human gene therapy or clinical diagnosis.



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