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70664 Benzonase® Nuclease, Purity > 99%

Effective viscosity reduction and removal of nucleic acids from protein solutions

Benzonase® Nuclease, Purity > 99% MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
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70664
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      Description
      OverviewBenzonase® Nuclease is a genetically engineered endonuclease from Serratia marcescens. It degrades all forms of DNA and RNA (single stranded, double stranded, linear and circular) while having no proteolytic activity. It is effective over a wide range of conditions and possesses an exceptionally high specific activity. The enzyme completely digests nucleic acids to 5′-monophosphate terminated oligonucleotides 2 to 5 bases in length (below the hybridization limit), which is ideal for removal of nucleic acids from recombinant proteins, enabling compliance with FDA guidelines for nucleic acid contamination. The ability of Benzonase to rapidly hydrolyze nucleic acids makes the enzyme an excellent choice for viscosity reduction to reduce processing time and increase yields of protein. For example, the enzyme is compatible with BugBuster® and PopCulture® Protein Extraction Reagents and can therefore be added along with these reagents to eliminate viscosity and remove nucleic acids from E. coli extracts.

      The enzyme consists of two subunits of 30 kDa each. It is functional between pH 6 and 10 and from 0-42°C and requires 1-2 mM Mg2+ for activation. The enzyme is also active in the presence of ionic and non-ionic detergents, reducing agents, PMSF (1 mM), EDTA (1 mM) and urea (relative activity depends on specific conditions). Activity is inhibited by > 150 mM monovalent cations, > 100 mM phosphate, > 100 mM ammonium sulfate, or > 100 mM guanidine HCl.

      Benzonase Nuclease is available in ultrapure (> 99% by SDS-PAGE) and pure (> 90%) grades at a standard concentration of 25-29 U/µl and at a high concentration (HC) of 250 U/µl. Both preparations are free of detectable protease and have specific activity > 1 × 106 U/mg protein. The > 99% purity grade is tested for endotoxins and contains < 0.25 EU/1000 units. The product is supplied in 50% glycerol. Store at -20°C.

      Total endotoxin: < 0.25 EU/1,000 units. Purity: > 99% by SDS-PAGE.
      Catalogue Number70664
      Brand Family Novagen®
      References
      Product Information
      Unit of DefinitionOne unit is defined as the amount of enzyme that causes a ΔA₂₆₀ of 1.0 in 30 minutes, which corresponds to complete digestion of 37 µg DNA.
      Quality LevelMQ300
      Applications
      Biological Information
      Purity> 99% by SDS-PAGE
      Physicochemical Information
      ContaminantsTotal endotoxin: < 0.25 EU/1000 units.
      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
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      70664-3CN 07790788052751

      Documentation

      Benzonase® Nuclease, Purity > 99% Certificates of Analysis

      TitleLot Number
      70664

      Brochure

      Title
      Bulk Product Guide
      Overnight Express Autoinduction Systems
      Protein Purification and Detection Tools

      Technical Info

      Title
      Benzonase®endonuclease for improved primary recovery in an E. coli-based process for Fab production

      Citations

      Title
    • Huaman, M.C., et al. 2008. Journal of Immunology 180, 1451.
    • Masip, L., et al. 2008. Journal of Biological Chemistry 283, 840.
    • Suzuki, C., et al. 2008. Procedings of the National Academy of Science 105, 3274.
    • Hervas-Stubbs, S., et al. 2007. Journal of Immunology 178, 2361.
    • Lisa Kercher, L., et al. 2007. Journal of Virology 81, 10340.
    • Kobayashi, S., et al. 2007. Journal of Biological Chemistry 282, 18407.
    • Lloyd-Burton, S.M., et al. 2007. Journal of Biological Chemistry 282, 9526.
    • Mingozzi, F., et al. 2007. Blood 110, 2334.
    • Nishiwaki, H., et al. 2007. Applied and Enviornmental Microbiology 73, 3404.
    • Norgett, E.E., et al. 2007. Journal of Biological Chemistry 282, 14421.
    • Oliveira, J.B., et al. 2007. Procedings of the National Academy of Science 104, 8953.
    • Park, M.-O., et al. 2007. Journal of Bacteriology 189, 7281.
    • Sukumar, N., et al. 2007. Journal of Bacteriology 189, 3695.
    • Cho, C.M-H., et al. 2006. Protein Engineering Design and Selection 19, 99.
    • Song, F., et al. 2006. Journal of Biological Chemistry 281, 11028.
    • Cashikar, A.G.,et al. 2005. Journal of Biological Chemistry 280, 23869.
    • Cho, S., et al. 2005. Molecular Endocrinology 19, 290.
    • Frankel, P., et al. 2005. European Molecular Biology Organization Journal 24, 54.
    • Han, W., et al. 2005. Journal of Biological Chemistry 280, 5089.
    • Johnsen, L., et al. 2005. Journal of Biological Chemistry 280, 19045.
    • Keating, S.M., et al. 2005. Journal of Immunology 175, 5675.
    • Kepple, K/V., et al. 2005. Proceedings of the National Academy of Sciences (USA) 102, 6867.
    • Kessler, t., et al. 2005. Clinical Cancer Research 11, 6317.
    • Kumaran, D., et al. 2005. Protein Science 14, 719.
    • Meyn, M.A., et al. 2005. Molecular Pharmacology 68, 1320.
    • Michelle A. Poirier, M.A., et al. 2005. Human Molecular Genetics 14, 765.
    • Vuola, J.M., et al. 2005. Journal of Immunology 174, 449.
    • Wu, T., et al. 2005. Cell 121, 235.
    • Yamakoshi, Y., et al. 2005. Journal of Biological Chemistry 280, 1552.
    • Zanghi, C.N., et al. 2005. Nucleic Acids Research 33, e160.
    • Kasim, V., et al. 2004. Nucleic Acids Research 32, e66.
    • Lunin, et al. 2004. Journal of Biological Chemistry 279, 23422.
    • Moy, S., et al. 2004. Journal of Structural and Functional Genomics 5, 103.
    • Nguyen, H., et al. 2004. Journal of Structural and Functional Genomics 5, 23.
    • Rizzo, M.A., et al. 2004. Nature Biotechnology 22, 445.
    • Murphy, M.B., et al. 2003. Nucleic Acids Research 31, e110.
    • Chan, W.W., et al. 2002. Biochimica et Biophysica Acta 1596, 1.
    • Huhtinen, K., et al. 2002. Journal of Biological Chemistry 277, 3424.
    • Lobel, L., et al. 2002. Protein Expression and Purification 25, 124.
    • Keri L.N. Mercer and David S. Weiss. 2002. Journal of Bacteriology 184, 904.
    • Peitz, M., et al. 2002. Procedings of the National Academy of Science 99, 4489.
    • Suarez, T., et al. 2002. Journal of Biological Chemistry 277, 21759.
    • Glick, E., et al. 2001. European Molecular Biology Organization Journal 20, 7303.
    • Hoffman, M., et al. 2001. Journal of Neurochemistry 78, 797.
    • Lobel, L.I., et al. 2001. Endocrine 14, 205.
    • Persad, S., et al. 2001. Journal of Biological Chemistry 276, 27462.
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      User Protocols

      Title
      TB261 Benzonase® Nuclease

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