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70746 Benzonase® Nuclease, Purity > 90%

Benzonase® Nuclease, Purity > 90% MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
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70746
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개요

Replacement Information

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카탈로그 번호 재고 정보패킹 포장 단위 가격(VAT 별도) 수량
70746-3CN
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      		 Glass bottle 10 ku
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      70746-4CN
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          		 Plastic ampoule 2.5 ku
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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: > 90% by SDS-PAGE
          Catalogue Number70746
          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
          PurityPurity: > 90% by SDS-PAGE.
          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 -20°C
          Do not freeze Ok to freeze
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications
          Global Trade Item Number
          카탈로그 번호 GTIN
          70746-3CN 07790788052805
          70746-4CN 04055977256949

          Documentation

          Benzonase® Nuclease, Purity > 90% MSDS

          타이틀

          물질안전보건자료(MSDS) 

          Benzonase® Nuclease, Purity > 90% Certificates of Analysis

          TitleLot Number
          70746

          Brochure

          Title
          Bulk Product Guide
          Protein Purification and Detection Tools

          Technical Info

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

          Citations

          타이틀
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        • Yasuo Yamakoshi, et al. (2005) Porcine dentin sialoprotein is a proteoglycan with glycosaminoglycan chains containing chondroitin 6-sulfate. Journal of Biological Chemistry 280, 1552-1560.
        • Christine N. Zanghi, et al. (2005) A simple method for displaying recalcitrant proteins on the surface of bacteriophage lambda. Nucleic Acids Research 33, e160.
        • Vivi Kasim, Makoto Miyagishi and Kazunari Taira. (2004) Control of siRNA expression using the Cre-loxP recombination system. Nucleic Acids Research 32, e66.
        • Vladimir V. Lunin, et al. (2004) The structure of the MAPK scaffold, MP1, bound to Its partner, p14 A complex with a critical role in endosomal MAP kinase signaling. Journal of Biological Chemistry 279, 23422-23430.
        • S. Moy, et al. (2004) Genome-scale expresion of proteins from Bacillus subtilis. Journal of Structural and Functional Genomics 5, 103-109.
        • Henry Nguyen, et al. (2004) An automated small-scale protein expression and purification screening provides beneficial information for protein production. Journal of Structural and Functional Genomics 5, 23-27.
        • Mark A. Rizzo, et al. (2004) An improved cyan fluorescent protein variant useful for FRET. Nature Biotechnology 22, 445-449.
        • Michael B. Murphy, et al. (2003) An improved method for the in vitro evolution of aptamers and applications in protein detection and purification. Nucleic Acids Research 31, e110-.
        • Wayne W. Chan, Steven L. Roderick and David E. Cohen. (2002) Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data. Biochimica et Biophysica Acta 1596, 1-5.
        • Kaisa Huhtinen, et al. (2002) The peroxisome proliferator-induced cytosolic type I acyl-CoA thioesterase (CTE-I) is a serine-histidine-aspartic acid α/β hydrolase. Journal of Biological Chemistry 277, 3424-3432.
        • Leslie Lobel, et al. (2002) Bacterial expression of a natively folded extracellular domain fusion protein of the hFSH receptor in the cytoplasm of Escherichia coli. Protein Expression and Purification 25, 124-133.
        • Keri L.N. Mercer and David S. Weiss. (2002) The Escherichia coli cell divisionn protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site. Journal of Bacteriology 184, 904-912.
        • Michael Peitz, et al. (2002) Ability of the hydrophobic FGF and basic TAT peptides to promote cellular uptake of recombinant Cre recombinase: a tool for efficient genetic engineering of mammalian genomes. Procedings of the National Academy of Science 99, 4489-4494.
        • Tatiana Suarez, Subhasis B. Biswas and Esther E. Biswas. (2002) Biochemical defects in retina-specific human ATP binding cassette transporter nucleotide binding domain 1 mutants associated with macular degeneration. Journal of Biological Chemistry 277, 21759-21767.
        • Eitan Glick, Kellie L. Vigna and Lawrence A. Loeb. (2001) Mutations in human DNA polymerase η motif II after bypass of DNA lesions. European Molecular Biology Organization Journal 20, 7303-7312.
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          User Protocols

          Title
          TB261 Benzonase® Nuclease

          관련 제품 및 어플리케이션

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          카테고리

          Life Science Research > Protein Sample Preparation > Protein Extraction > Nucleases & Enhancers