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  Benzonase® Nuclease, Purity > 90%
Cat. No. 70746  
All Categories » Novagen » Protein Expression, Purification, and Detection » Protein Extraction » Benzonase® Nuclease
Benzonase® Nuclease
Effective viscosity reduction and removal of nucleic acids from protein solutions
 
Benzonase® 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 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 as a 0.2 µm filtered solution in 50% glycerol. Store at -20°C.

 
 
Product Description

Purity: > 90% by SDS-PAGE.

Unit Activity: One unit is defined as the amount of enzyme that causes a DA260 of 1.0 in 30 minutes, which corresponds to complete digestion of 37 µg DNA.  

Need additional information about this product? Email our Technical Service department at: novatech@novagen.com

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E. coli cells BL21(DE3) containing a pET construct were suspended in BugBuster reagent (5 ml/g wet weight). Aliquots of the suspension were treated with the indicated amounts of Benzonase for 10 min at room temperature, centrifuged at 350 × g for 3 min and photographed.

Related Products:
70664: Benzonase® Nuclease, Purity > 99%
70746: Benzonase® Nuclease, Purity > 90%
71205: Benzonase® Nuclease HC, Purity > 90%
71206: Benzonase® Nuclease HC, Purity > 99%

Related Literature:

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70746: Benzonase® Nuclease, Purity > 90% - English
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All Categories » Novagen » Protein Expression, Purification, and Detection » Protein Extraction » Benzonase® Nuclease

Selected Citations:
  1. Sandra Hervas-Stubbs, et al. (2007) Insect baculoviruses strongly potentiate adaptive immune responses by inducing type I IFN. Journal of Immunology 178, 2361-2369.
  2. Samantha M. Lloyd-Burton, et al. (2007) Regulation of Ins(1,4,5)P3 3-kinases by calcium and localization in cells. Journal of Biological Chemistry 282, 9526-9535.
  3. Federico Mingozzi, et al. (2007) Modulation of tolerance to the transgene product in a nonhuman primate model of AAV-mediated gene transfer to liver. Blood 110, 2334-2341.
  4. Joao B. Oliveira, et al. (2007) NRAS mutation causes a human autoimmune lymphoproliferative syndrome. Procedings of the National Academy of Science 104, 8953-8958.
  5. Myong-Ok Park, Taeko Mizutani and Patrik R. Jones. (2007) Glyceraldehyde-3-phosphate ferredoxin oxidoreductase from Methanococcus maripaludis. Journal of Bacteriology 189, 7281-7289.
  6. Sehyung Cho, et al. (2005) Glucocorticoid receptor ligand binding domain is sufficient for the modulation of glucocorticoid induction properties by homologous receptors, coactivator transcription intermediary factor 2, and ubc9. Molecular Endocrinology 19, 290-311.
  7. Paul Frankel, et al. (2005) RalA interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activity. European Molecular Biology Organization Journal 24, 54-62.
  8. Weiping Han, et al. (2005) C-terminal ECFP Fusion Impairs Synaptotagmin 1 Function: crowding out synaptotagmin 1. Journal of Biological Chemistry 280, 5089-5100.
  9. Line Johnsen, et al. (2005) 1.6 Ĺ crystal structure of EntA-Im: A bacterial immunity protein conferring immunity to the antimicrobial activity of the pediocin-like bacteriocin enterocin A. Journal of Biological Chemistry 280, 19045-19050.
  10. Sheila M. Keating, et al. (2005) Durable human memory T cells quantifiable by cultured enzyme-linked immunospot assays are induced by heterologous prime boost immunization and correlate with protection against malaria. Journal of Immunology 175, 5675-5680.

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