524739 Phosphodiesterase 10A2, His•Tag®, Human, Recombinant, S. frugiperda

524739
View Pricing & Availability

Overview

Replacement Information

Key Specifications Table

Pricing & Availability

Catalog Number AvailabilityPackaging Qty/Pack Price Quantity
524739-10U
Retrieving availability...
Limited AvailabilityLimited Availability
Stocked 
Discontinued
Limited Quantities Available
Available
    Remaining : Will advise
      Remaining : Will advise
      Will advise
      Contact Customer Service
      Contact Customer Service

      Plastic ampoule 10 u
      Retrieving price...
      Price could not be retrieved
      Minimum Quantity needs to be mulitiple of
      Upon Order Completion More Information
      You Saved ()
       
      Request Pricing
      Description
      OverviewFull-length, recombinant, human, phosphodiesterdase 10A2 (accession no. 10A2) fused at the N-terminus to a His•Tag7reg; sequence and expressed in S. frugiperda insect cells using a baculovirus expression system. Supplied as a partially purified preparation of catalytically active enzyme.
      Catalogue Number524739
      Brand Family Calbiochem®
      SynonymsPDE10A2
      References
      ReferencesKotera, J., et. al. 2004. J. Biol. Chem. 279, 4366.
      Fujishige K., et. al. 1999. Eur. J. Biochem. 266, 1118.
      Kotera, J., et. al. 1999. Biochem. Biophys. Res. Commun. 261, 551.
      Product Information
      Activity≥ 0.25 U/µl
      Unit of DefinitionOne unit is defined as the amount of enzyme required to convert 1 µmol cAMP to AMP per min at 30°C, pH 7.5.
      EC number3.1.4.17
      FormLiquid
      FormulationIn RIPA buffer (150 mM NaCl, 10 mM Tris-HCl, 1% NP-40), pH 8.3.
      Quality LevelMQ100
      Applications
      Biological Information
      Physicochemical Information
      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

      Documentation

      Phosphodiesterase 10A2, His•Tag®, Human, Recombinant, S. frugiperda SDS

      Title

      Safety Data Sheet (SDS) 

      Phosphodiesterase 10A2, His•Tag®, Human, Recombinant, S. frugiperda Certificates of Analysis

      TitleLot Number
      524739

      References

      Reference overview
      Kotera, J., et. al. 2004. J. Biol. Chem. 279, 4366.
      Fujishige K., et. al. 1999. Eur. J. Biochem. 266, 1118.
      Kotera, J., et. al. 1999. Biochem. Biophys. Res. Commun. 261, 551.
      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.

      Revision18-August-2010 JSW
      SynonymsPDE10A2
      DescriptionFull-length, recombinant, human, phosphodiesterdase 10A2 (accession no. 10A2) fused at the N-terminus to a His•Tag7reg; sequence and expressed in S. frugiperda insect cells using a baculovirus expression system. Supplied as a partially purified preparation of catalytically active enzyme.
      FormLiquid
      FormulationIn RIPA buffer (150 mM NaCl, 10 mM Tris-HCl, 1% NP-40), pH 8.3.
      EC number3.1.4.17
      Activity≥ 0.25 U/µl
      Unit definitionOne unit is defined as the amount of enzyme required to convert 1 µmol cAMP to AMP per min at 30°C, pH 7.5.
      Storage ≤ -70°C
      Avoid freeze/thaw
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Toxicity Standard Handling
      ReferencesKotera, J., et. al. 2004. J. Biol. Chem. 279, 4366.
      Fujishige K., et. al. 1999. Eur. J. Biochem. 266, 1118.
      Kotera, J., et. al. 1999. Biochem. Biophys. Res. Commun. 261, 551.