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208707 Ca2+/Calmodulin Kinase II, Rat Brain

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

Synonymes: CaM Kinase II

208707
  
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      Aperçu

      Replacement Information
      Description
      Overview

      This product has been discontinued.



      We are currently only offering Ca2+/Calmodulin Kinase II, α-Subunit, Rat, Recombinant, Spodoptera frugiperda (Cat. No. 208706) as a possible alternative. Please read the alternative product documentation carefully and contact technical service if you need additional information.






      Native Ca2+/calmodulin kinase II from rat brain. A multi-functional calcium and calmodulin-dependent protein kinase that regulates a number of cellular functions including neurotransmitter synthesis and release, gene expression, ion channel function, carbohydrate metabolism, cytoskeletal function, and Ca2+-homeostasis. Reduced levels are reported following ischemia and neuronal injury. Consists of subunits of M.W. 50,000 and 58,000 - 60,000 in a 3:1 ratio.
      Catalogue Number208707
      Brand Family Calbiochem®
      SynonymsCaM Kinase II
      References
      ReferencesTakeuchi, Y., et al. 2000. J. Neurochem. 74, 2557.
      Enslen, H., and Soderling, T.R. 1994. J. Biol. Chem. 269, 20872.
      Lisman, J. 1994. Trends Neurosci. 17, 406.
      Bading, H., et al. 1993. Science 260, 181.
      Machu, T.K., et al. 1993. J. Neurochem. 61, 375.
      Shackelford, D.A., et al. 1993. J. Neurochem. 61, 738.
      Hanson, P.I., and Schulman, H. 1992. Annu. Rev. Biochem. 61, 559.
      Browning, M.D., et al. 1990. Proc. Natl. Acad. Sci. USA 87, 1315.
      Patton, B.L., et al. 1990. J. Biol. Chem. 265, 11204.
      Kelly, P.T., and Shenolikar, S. 1987. Methods Enzymol. 139, 690.
      Product Information
      CAS number9026-43-1
      Unit of DefinitionOne unit is defined as the amount of enzyme that will transfer 1.0 µmol phosphate to synapsin I per min at 30°C.
      FormLiquid
      FormulationIn 25 mM Tris-HCl, 10 mM DTT, 500 µM EDTA, 10 µM AEBSF, 100 µg/ml leupeptin, 50% glycerol, pH 7.5.
      Applications
      Biological Information
      Purity≥95% by SDS-PAGE
      Specific Activity≥1.0 µmol/min/mg protein
      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
      Global Trade Item Number
      Référence GTIN
      208707 0

      Documentation

      Ca2+/Calmodulin Kinase II, Rat Brain Certificats d'analyse

      TitreNuméro de lot
      208707

      Références bibliographiques

      Aperçu de la référence bibliographique
      Takeuchi, Y., et al. 2000. J. Neurochem. 74, 2557.
      Enslen, H., and Soderling, T.R. 1994. J. Biol. Chem. 269, 20872.
      Lisman, J. 1994. Trends Neurosci. 17, 406.
      Bading, H., et al. 1993. Science 260, 181.
      Machu, T.K., et al. 1993. J. Neurochem. 61, 375.
      Shackelford, D.A., et al. 1993. J. Neurochem. 61, 738.
      Hanson, P.I., and Schulman, H. 1992. Annu. Rev. Biochem. 61, 559.
      Browning, M.D., et al. 1990. Proc. Natl. Acad. Sci. USA 87, 1315.
      Patton, B.L., et al. 1990. J. Biol. Chem. 265, 11204.
      Kelly, P.T., and Shenolikar, S. 1987. Methods Enzymol. 139, 690.
      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.

      Revision04-August-2008 RFH
      SynonymsCaM Kinase II
      DescriptionNative Ca2+/calmodulin kinase II from rat brain. Multifunctional calcium and calmodulin dependent protein kinase that regulates a number of cellular functions including, neurotransmitter synthesis and release, gene expression, ion channel function, carbohydrate metabolism, cytoskeletal function, and calcium homeostasis. Reduced levels are reported following ischemia and neuronal injury. Consists of subunits of M.W. 50,000 and 58,000-60,000 in a 3:1 ratio. Phosphorylates a number of substrates including calcineurin, CRE-binding protein, IP3 receptor, intermediate filaments, microtubule-associated proteins, ribosomal protein S6, synapsin I, tyrosine hydroxylase, and tryptophan hydroxylase.
      FormLiquid
      FormulationIn 25 mM Tris-HCl, 10 mM DTT, 500 µM EDTA, 10 µM AEBSF, 100 µg/ml leupeptin, 50% glycerol, pH 7.5.
      Recommended reaction conditions
      Reaction Mixture: 50 mM HEPES, pH 7.4, 5 mM MgCl2, 0.3 mM CaCl2, 30 µg/ml calmodulin, 0.2 mg/ml synapsin I, 0.6 µg/ml CaM Kinase II, and 50 µM ATP (1-10 µCi of [γ-32P]ATP). Samples are typically incubated for 2 min at 22-30°C.
      CAS number9026-43-1
      Purity≥95% by SDS-PAGE
      Specific activity≥1.0 µmol/min/mg protein
      Unit definitionOne unit is defined as the amount of enzyme that will transfer 1.0 µmol phosphate to synapsin I per min at 30°C.
      Storage Avoid freeze/thaw
      ≤ -70°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Toxicity Standard Handling
      ReferencesTakeuchi, Y., et al. 2000. J. Neurochem. 74, 2557.
      Enslen, H., and Soderling, T.R. 1994. J. Biol. Chem. 269, 20872.
      Lisman, J. 1994. Trends Neurosci. 17, 406.
      Bading, H., et al. 1993. Science 260, 181.
      Machu, T.K., et al. 1993. J. Neurochem. 61, 375.
      Shackelford, D.A., et al. 1993. J. Neurochem. 61, 738.
      Hanson, P.I., and Schulman, H. 1992. Annu. Rev. Biochem. 61, 559.
      Browning, M.D., et al. 1990. Proc. Natl. Acad. Sci. USA 87, 1315.
      Patton, B.L., et al. 1990. J. Biol. Chem. 265, 11204.
      Kelly, P.T., and Shenolikar, S. 1987. Methods Enzymol. 139, 690.