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539514 Protein Phosphatase, Lambda, Recombinant, E. coli

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      概要

      Replacement Information
      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
      カタログ番号 GTIN
      539514 0

      Documentation

      Protein Phosphatase, Lambda, Recombinant, E. coli (M)SDS

      タイトル

      英語版製品安全データシート((M)SDS) 

      Protein Phosphatase, Lambda, Recombinant, E. coli 試験成績書(CoA)

      タイトルロット番号
      539514

      参考資料

      参考資料の概要
      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.

      カタログ

      タイトル
      Protein Phosphatases Technical Bulletin
      データシート

      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.