Lambda Protein Phosphatase02-30020,000 U(400U/µl)

02-300-5

5 x 20,000 U(400U/µl)

Storage : Store at -80℃. Avoid freeze-thaw cycles.
Product: Functional full-length recombinant λProtein Phosphatase (λ-PPase) expressed inE.coli. It is a Mn+2-dependent protein phosphatase with activity towards phosphorylated
serine, threonine, tyrosine and histidine residues.

It is the 221 amino-acid product ofORF221 open reading frame on bacteriophage lambda (1, 2). This product is an intact
enzyme of high quality without tag.
Applications: λ-PPase can be used to release phosphate groups from phosphorylated serine,threonine, tyrosine and histidine residues in proteins (2).
proteins are dephosphorylated at different rates.

It should be noted that different

Optimal reaction temperature is 30℃.

Inclusion of protease inhibitor cocktail and shortest incubation time is desired when assays
are done with crude samples.
Form: 400 U/ul λ-PPase in 50mM HEPES (pH 7.5), 100mM NaCl, 2mM dithiothreitol,
0.1 mM MnCl2, 0.1mM EDTA, 50% glycerol, 0.01% Brij 35.
Activity: 400 U/ul, where one unit is defined as the amount of enzyme that hydrolyzes
1 nmole of p-nitrophenyl phosphate per minute at 30 ℃ .

Unit definition assays are

performed with 50mM p-nitrophenyl phosphate in λ-PPase buffer, supplemented with 2mM MnCl2 in a 50 ul reaction.
Specific Activity: ~400,000 U/mg
Purity: Greater than 95% as determined by SDS-PAGE (CBB staining)that contains no detectable protease activity
Reagents Supplied with Enzyme:(1)10 x λ-PPase Reaction Buffer: [500mM Tris-HCl (pH 7.6), 1M NaCl, 20mM
dithiothreitol, 1mM EDTA, 0.1% Brij 35](2)10 x Mn2+ (20 mM MnCl2)（02-Lpb1ml）（02-Lmn1ml）

Data Link: UniProtKB/Swiss-Prot P03772 (PP_LAMBD)

Fig.1 SDS-PAGE of  -75

Protein Phosphatase

5Phosphatase

32

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Fig.2Dephosphorylation of phospho -NPM1 protein by incubation with
λprotein phosphatase in vitro.
50 kDaHeLa cells treated with Nocodazole
was lysed, and NPM1 protein was

Phospho-NPM1
NPM1 33 kDa

immunoprecipitedwithantibody.

precipitateThe

anti-NPM1
wassuspended in 50 ul of λ protein

25 kDaphosphatase reaction buffer added with
5 ul of the protein phosphatase andincubated at 30 ℃ for the indicatedtime (min). The reaction products wereanalyzed by western blotting.
Data were kindly provided by Prof. T.
Reference: This product has been used in the following publications.
at Shimane
Univ. between
School of1.Tojima T et al. Steering neuronal growth cones Uranoby shifting
the imbalance
Medicine.
exocytosis and endocytosis. J Neurosci. 2014 May 21;34(21):7165-78.
PMID: 24849351
2.Moriyama T et al.SUMO-modification and elimination of the active DNA demethylation
enzyme TDG in cultured human cells. Biochem Biophys Res Commun. 2014 May
9;447(3):419-24. PMID: 24727457
3.Yang CC et al. Claspin recruits Cdc7 kinase for initiation of DNA replication in human cells.
Nature Commun. 2016, 7: 12135. PMID: 27401717
4. Tomii S et al. Cortical Actin Alteration at the Matrix-Side Cytoplasm in Lung
Adenocarcinoma Cells and Its Significance in Invasion. Pathobiology.2017; 84(4):171183. PMID: 28002815
5.Honda T & Inui M. PDZRN3 regulates differentiation of myoblasts into myotubes throughtranscriptional and posttranslational control of Id2. J. Cell Physiol. 2019, 234: 2963-2972.
PMID: 30066954
Useful References:
1. Cohen PTW & Cohen P (1989) “Discovery of a protein phosphatase activity
encoded in the genome of bacteriophage .” 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
Please note: All products are FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC
PROCEDURES. NOT FOR MILITARY USE.
BioAcademia,Inc.

Tel. 81-6-6877-2335

Fax. 81-6-6877-2336

info@bioacademia.co.jp

https://www.bioacademia.co.jp/en/