71049 Proteinase K Solution, 600 mAU/ml

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      Glass bottle 10 ml
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      OverviewProteinase K is a highly active 28,904-Da serine protease isolated from the fungus Tritirachium album. The enzyme exhibits broad cleavage specificity on native and denatured proteins and is widely used in the purification of DNA and RNA. Its activity is increased in the presence of denaturants such as SDS (1%) and elevated temperature (50-60°C). The recommended working concentration is 50-100 µg/ml for protein removal and enzyme inactivation, and up to 2 mg/ml for tissue treatment. The Proteinase K, Lyophilized powder can be prepared as a 20 mg/ml stock solution in water and stored in aliquots at -20°C. The enzyme is also available as a ready-to-use concentrated stock solution (600 mAU/ml) that is convenient for routine use in most applications. 1 mg of Proteinase K is the equivalent of 30 mAU (AU = Anson unit). The Novagen Proteinase K products are free of detectable DNase and RNase
      Catalogue Number71049
      Brand Family Novagen®
      Product Information
      Unit of DefinitionOne AU (AU = Anson unit) is defined as the amount of enzyme that liberates 1.0 µmol (181 µg) of tyrosine from casein per minute at pH 7.5 at 37°C.
      Biological Information
      Physicochemical Information
      ContaminantsFree of detectable DNase and RNase.
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Shipped with Blue Ice or with Dry Ice
      Toxicity Harmful
      Storage -20°C
      Do not freeze Ok to freeze
      Packaging Information
      Transport Information
      Supplemental Information


      Proteinase K Solution, 600 mAU/ml Certificates of Analysis

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      The Complete Molecular Biology Toolkit - Expert workflow solutions from DNA cloning to protein expression


    • Shannon M. Anderson, et al. (2007) New markers for murine memory B cells that define mutated and unmutated subsets. Journal of Experimental Medicine 204, 2103-2114.
    • Andrew A. Horwitz, et al. (2007) ATP-induced structural transitions in PAN, the proteasome-regulatory ATPase complex in Archaea. Journal of Biological Chemistry 282, 22921-22929.
    • User Protocols

      TB271 Proteinase K

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      Life Science Research > Proteins and Enzymes > Other Enzymes