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539493 PP1, α-Isoform, Rabbit Muscle, Recombinant, E. coli

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539493
  
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      Übersicht

      Replacement Information
      Description
      Overview

      This product has been discontinued.



      Recombinant, rabbit, Mn2+-dependent catalytic subunit of the α-isoform of protein phosphatase 1 expressed in E. coli. Hydrolyzes the phosphate groups on serine and threonine residues and has also been known to hydrolyze phosphates on tyrosine residues. Assists in tobacco mosaic virus-mediated programmed cell death.

      Catalogue Number539493
      Brand Family Calbiochem®
      SynonymsProtein Phosphatase 1, α-Isoform, Phosphorylase Phosphatase
      References
      ReferencesDunigan, D.D., and Madlener, J.C. 1995. Virology 207, 460.
      Zhang, Z., et al. 1993. Mol. Cell. Biochem. 127, 113.
      Zhang, A.J., et al. 1992. J. Biol. Chem. 267, 1484.
      Product Information
      Activity≥500 units/ml
      Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 nmol of pNPP per minute at 30°C, pH 7.0.
      FormLiquid
      FormulationIn 200 mM NaCl, 50 mM HEPES, 2.5 mM DTT, 1 mM MnCl₂, 0.1 mM EGTA, 50% glycerol, 0.025% TWEEN®-20 Detergent, pH 7.0.
      Applications
      Biological Information
      Specific Activity13,500 units/mg
      Physicochemical Information
      ContaminantsProtease: 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
      Bestellnummer GTIN
      539493 0

      Documentation

      PP1, α-Isoform, Rabbit Muscle, Recombinant, E. coli Analysenzertifikate

      TitelChargennummer
      539493

      Literatur

      Übersicht
      Dunigan, D.D., and Madlener, J.C. 1995. Virology 207, 460.
      Zhang, Z., et al. 1993. Mol. Cell. Biochem. 127, 113.
      Zhang, A.J., et al. 1992. J. Biol. Chem. 267, 1484.

      Broschüre

      Titel
      Protein Phosphatases Technical Bulletin
      Datenblatt

      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.

      Revision04-September-2008 RFH
      SynonymsProtein Phosphatase 1, α-Isoform, Phosphorylase Phosphatase
      DescriptionRecombinant, rabbit, Mn2+-dependent catalytic subunit of the α-isoform of protein phosphatase 1 expressed in E. coli. Hydrolyzes the phosphate groups on serine and threonine residues, and has also been known to hydrolyze phosphates on tyrosine residues. Assists in tobacco mosaic virus-mediated programmed cell death.
      FormLiquid
      FormulationIn 200 mM NaCl, 50 mM HEPES, 2.5 mM DTT, 1 mM MnCl₂, 0.1 mM EGTA, 50% glycerol, 0.025% TWEEN®-20 Detergent, pH 7.0.
      Recommended reaction conditions50 mM Tris-HCl, 5 mM DTT, 200 µM MnCl2, 100 µM EDTA, and 200 µg/ml BSA, pH 7.0. 50 mM caffeine is required if phosphorylase is the substrate.
      ContaminantsProtease: none detected
      Specific activity13,500 units/mg
      Activity≥500 units/ml
      Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 nmol of pNPP per minute at 30°C, pH 7.0.
      Storage Avoid freeze/thaw
      ≤ -70°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°c).
      Toxicity Standard Handling
      ReferencesDunigan, D.D., and Madlener, J.C. 1995. Virology 207, 460.
      Zhang, Z., et al. 1993. Mol. Cell. Biochem. 127, 113.
      Zhang, A.J., et al. 1992. J. Biol. Chem. 267, 1484.