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70746 Benzonase® Nuclease, Purity > 90%

Benzonase® Nuclease, Purity > 90%: MSDS (material safety data sheet) o SDS, certificato d’analisi (CoA) e certificato di qualità (CoQ), dossier, brochure e altri documenti disponibili.
70746
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Panoramica

Replacement Information

Products

Numero di catalogoConfezionamento Qtà/conf
70746-3 Bottiglia di vetro 10 ku
70746-4 Fiala di plastica 2.5 ku
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
Numero di catalogo GTIN
70746-3 07790788052805
70746-4 04055977256949

Documentation

Benzonase® Nuclease, Purity > 90% MSDS

Titolo

Scheda di sicurezza (MSDS) 

Benzonase® Nuclease, Purity > 90% Certificati d'Analisi

TitoloNumero di lotto
70746

Brochure

Titolo
Bulk Product Guide
Protein Purification and Detection Tools

Informazioni tecniche

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

Citazioni

Titolo
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  • Jenni M. Vuola, et al. (2005) Differential immunogenicity of various heterologous prime-boost vaccine regimens using DNA and viral vectors in healthy volunteers. Journal of Immunology 174, 449-455.
  • 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.
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  • 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.
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  • 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.
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  • Marcel Hoffman, et al. (2001) Differential capacities of the RGS1, RGS16 and RGS-GAIP regulators of G protein signaling to enhance α2A-adrenoreceptor agonist-stimulated GTPase activity of Go1α. Journal of Neurochemistry 78, 797-806.
  • L.I. Lobel, et al. (2001) High-level bacterial expression of a natively folded, soluble extracellular domain fusion protein of the human luteinizing hormaone/ chorionic gonadotropin receptor in the cytoplasm of Escherichia coli. Endocrine 14, 205-212.
  • Sujata Persad, et al. (2001) Regulation of protein kinase B/ Akt-serine 473 phosphorylation by integrin-linked kinase. Journal of Biological Chemistry 276, 27462-27469.
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    Protocolli per l'uso

    Titolo
    TB261 Benzonase® Nuclease