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324825 EPAC2 cAMP Binding Domain, GST-Fusion, Human, Recombinant, E. coli

FDS (Fiches de données de sécurité), certificats d’analyse (CoA) et de qualité (CoQ), dossiers, brochures et autres documents disponibles.
324825
  
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      Aperçu

      Replacement Information
      Description
      Overview

      This product has been discontinued.





      Recombinant, human EPAC2 (Exchange Protein dirctly Activated by cAMP) consisting of amino acids 302-470 expressed in E. coli. EPAC2 is a guanine nucleotide exchange factor (GEF) that activates Rap GTPase upon bing to cAMP. Supplied as a partially purified preparation of catalytically active enzyme useful for binding and activity assays.
      Catalogue Number324825
      Brand Family Calbiochem®
      Application Data
      cAMP binding to EPAC2
      References
      ReferencesBos, J.L., 2006. Trends Biochem Sci. 31, 680.
      McPhee. I., et al. 2005. Biochem Soc Trans. 33, 1330.
      Product Information
      FormLiquid
      FormulationIn 150 mM NaCl, 10 mM Tris, 0.1% NP-40, pH 8.3.
      Applications
      Biological Information
      Biological activityEC₅₀ of cAMP binding: ≤1.5 µM
      Physicochemical Information
      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 +2°C to +8°C
      Do not freeze Ok to freeze
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Référence GTIN
      324825 0

      Documentation

      EPAC2 cAMP Binding Domain, GST-Fusion, Human, Recombinant, E. coli Certificats d'analyse

      TitreNuméro de lot
      324825

      Références bibliographiques

      Aperçu de la référence bibliographique
      Bos, J.L., 2006. Trends Biochem Sci. 31, 680.
      McPhee. I., et al. 2005. Biochem Soc Trans. 33, 1330.
      Fiche technique

      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.

      Revision23-June-2010 JSW
      Application Data
      cAMP binding to EPAC2
      DescriptionRecombinant, human EPAC2 (Exchange Protein dirctly Activated by cAMP) consisting of amino acids 302-470 expressed in E. coli. EPAC2 is a guanine nucleotide exchange factor (GEF) that activates Rap GTPase upon binding to cAMP. Supplied as a partially purified preparation of catalytically active enzyme useful for binding and activity assays.
      FormLiquid
      FormulationIn 150 mM NaCl, 10 mM Tris, 0.1% NP-40, pH 8.3.
      Recommended reaction conditions
      Activity and Inhibition Assay

      Materials Required •EPAC Buffer: 50 mM Tris, 50 mM NaCl, 5% Glycerol, pH 7.4 •96 well plates: Griener 655075, white •Ysi beads: Perkin Elmer RPNQ0033, stock concentration of 50 mg/5ml in 50 mM Tris, 0.1% Sodium Azide, pH 7.4 • 3H-cAMP • Compound of choice for inhibition: Dilute to desired concentration.
      Protocol 1. Perform serial dilutions of EPAC2 protein to determine optimum concentration per well. 2. Make a mixture of EPAC2 protein and EPAC Buffer to a total volume of 4 ml. The ratio depends on amount of protein added; i.e. 200µl EPAC2 protein and 3.8 ml EPAC Buffer/100µg Ysi beads (1 ml/plate). 3. Make 3H-cAMP to 1.5µCi/ml in EPAC Buffer. 4. Add 11µl compound. 5. Add 50µl EPAC2 protein/EPAC buffer/ 10 µg Ysi beads, while shaking to stop the beads from settling. 6. Add 50µl 3H-cAMP. 7. Incubate on shaker for 30 min. 8. Read on a scintillation counter.
      Biological activityEC₅₀ of cAMP binding: ≤1.5 µM
      Storage +2°C to +8°C
      Do Not Freeze Ok to freeze
      Toxicity Standard Handling
      ReferencesBos, J.L., 2006. Trends Biochem Sci. 31, 680.
      McPhee. I., et al. 2005. Biochem Soc Trans. 33, 1330.