Millipore Sigma Vibrant Logo

119186 ATP Sulfurylase, Saccharomyces cerevisiae

MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
119186
  
Retrieving price...
Price could not be retrieved
Minimum Quantity is a multiple of
Maximum Quantity is
Upon Order Completion More Information
You Saved ()
 
—
Request Pricing
—
Limited Availability Limited Availability
In Stock 
Discontinued
Limited Quantities Available
Availability to be confirmed
    Remaining : Will advise
      Remaining : Will advise
      Will advise
      Contact Customer Service
      Contact Customer Service

       

      Contact Customer Service

      Overview

      Replacement Information
      Description
      Overview

      This product has been discontinued.



      We apologize for the inconvenience, but we do not currently have an alternative product.






      Native ATP sulfurylase. Isolated from Baker’s yeast. A key enzyme in the activation of inorganic sulfate required for enzymatic sulfation. Useful for the synthesis of PAPS (Cat. No. 118410).
      Catalogue Number119186
      Brand Family Calbiochem®
      References
      ReferencesHawes, C.S., and Nicholas, D.J. 1973. Biochem. J. 133, 541.
      Product Information
      CAS number9012-39-9
      Unit of DefinitionOne unit is defined as the amount of enzyme that will catalyze the formation of 1.0 µmol ATP from APS and inorganic pyrophosphate per min at 30°C, pH 8.0.
      EC number2.7.7.4
      FormLyophilized
      FormulationLyophilized from 20 mM citrate, pH 7.5.
      Applications
      Biological Information
      Specific Activity≥5 units/mg protein
      Physicochemical Information
      ContaminantsAPS Kinase, ATPase, inorganic pyrophosphatase, phosphatase: ≤1%
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Blue Ice Only
      Toxicity Standard Handling
      Storage -20°C
      Do not freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable up to 3 months at -20°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      119186 0

      Documentation

      ATP Sulfurylase, Saccharomyces cerevisiae Certificates of Analysis

      TitleLot Number
      119186

      References

      Reference overview
      Hawes, C.S., and Nicholas, D.J. 1973. Biochem. J. 133, 541.
      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.

      Revision08-April-2008 RFH
      Description

      This product has been discontinued.

      We apologize for the inconvenience, but we do not currently have an alternative product.





      Native ATP sulfurylase. Isolated from Baker's Yeast. A key enzyme in the activation of inorganic sulfate required for enzymatic sulfation. Useful for the synthesis of PAPS (Cat. No. 118410).
      FormLyophilized
      FormulationLyophilized from 20 mM citrate, pH 7.5.
      Recommended reaction conditions50 mM Tris-HCl, 20 mM MgCl2, pH 8.0.
      CAS number9012-39-9
      EC number2.7.7.4
      ContaminantsAPS Kinase, ATPase, inorganic pyrophosphatase, phosphatase: ≤1%
      Specific activity≥5 units/mg protein
      Unit definitionOne unit is defined as the amount of enzyme that will catalyze the formation of 1.0 µmol ATP from APS and inorganic pyrophosphate per min at 30°C, pH 8.0.
      Storage -20°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable up to 3 months at -20°C.
      Toxicity Standard Handling
      ReferencesHawes, C.S., and Nicholas, D.J. 1973. Biochem. J. 133, 541.