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539514 Protein Phosphatase, Lambda, Recombinant, E. coli

MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Protein Phosphatase, Lambda

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539514
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Overview

Replacement Information

Products

Catalog NumberPackaging Qty/Pack
539514-20KU Plastic ampoule 20 ku
Description
OverviewRecombinant 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.
Note: 1 KU = 1000 units.
Catalogue Number539514
Brand Family Calbiochem®
SynonymsProtein Phosphatase, Lambda
References
ReferencesZhuo, 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.
Product Information
Activity≥400,000 units/ml.
Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 nmol of <i>p</i>NPP 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.
FormLiquid
FormulationIn 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.
Quality LevelMQ100
Applications
Biological Information
Purity≥95% by SDS-PAGE
Physicochemical Information
ContaminantsProtease activity: none detected
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Dry Ice Only
Toxicity Standard Handling
Storage ≤ -70°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalog Number GTIN
539514-20KU 04055977269239

Documentation

Protein Phosphatase, Lambda, Recombinant, E. coli SDS

Title

Safety Data Sheet (SDS) 

Protein Phosphatase, Lambda, Recombinant, E. coli Certificates of Analysis

TitleLot Number
539514

References

Reference overview
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.

Brochure

Title
Protein Phosphatases Technical Bulletin
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision01-April-2009 JSW
SynonymsProtein Phosphatase, Lambda
DescriptionRecombinant 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.
FormLiquid
FormulationIn 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.
Recommended reaction conditions50 mM Tris-HCl, 5 mM DTT, 2 mM MnCl2, 100 µg/ml BSA, pH 7.8.
Purity≥95% by SDS-PAGE
ContaminantsProtease activity: none detected
Activity≥400,000 units/ml.
Unit definitionOne 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.
SolubilityFurther dilute in 50 mM Tris-HCl, pH 7.8, 5 mM DTT, 2 mM MnCl₂, and 100 µg/ml BSA.
Storage Avoid freeze/thaw
≤ -70°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Toxicity Standard Handling
ReferencesZhuo, 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.