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目录产品 » Benz-Neburase™, tag-free
Benz-Neburase™, Tag-free

Lane M: DNA marker
Lane 1: PCR product
Lane 2: GenScript Benz-Neburase™, tag-free + PCR product
Lane 3: Competitor endonuclease+ PCR product
Lane 4: Genomic DNA
Lane 5: GenScript Benz-Neburase™, tag-free + Genomic DNA
Lane 6: Competitor endonuclease + Genomic DNA
Lane 7: Plasmid DNA
Lane 8: GenScript Benz-Neburase™, tag-free + Plasmid DNA
Lane 9: Competitor endonuclease + Plasmid DNA
Lane 10: RNA
Lane 11: GenScript Benz-Neburase™, tag-free + RNA
Lane 12: Competitor endonuclease + RNA

Benz-Neburase™, Tag-free

Lane M:SDS-PAGE marker
Lane R:Reducing (R)
Lane N:Non-reducing (NR)
Purity: > 95% as analyzed by SDS-PAGE

Benz-Neburase™, tag-free

The Benz-Neburase™ is an endonuclease capable of removing all forms of DNA and RNA, including double stranded, single stranded, linearized, and circular forms.
Z03695
¥392

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Expression System E.coli
Species Serratia Marcescen 
Tag Tag-free
Theoretical Molecular Weight 27.5 kDa
Biological Activity ≥ 1.1×106 U/mg
One unit of Benz-Neburase, tag-free is defined as the amount of enzyme for a ∆A260 of 1.0 (equivalent to the complete digestion of 37μg DNA) in 30 min.
Formulation Supplied as a solution of 20 mM Tris-HCl, 2 mM MgCl2, 20 mM NaCl, 50% Glycerol, pH 8.0.
Apparent Molecular Weight ~27.5 kDa, on SDS-PAGE under reducing conditions
Storage & Stability This product remains stable for up to 2 weeks at 4 °C or up to 24 months at -20 °C.
Avoid repeated freeze-thaw cycles.
Do not store below -20 °C!

The Benz-Neburase™ is an endonuclease capable of removing all forms of DNA and RNA, including double stranded, single stranded, linearized, and circular forms. The Benz-Neburase is commonly used in biopharmaceutical production such as vaccine, viral vector, gene and cell therapy manufacturing facilities.
The activity of Benz-Neburase™, tag-free requires 1-2 mM Mg2+.

Purity ≥ 95% as analyzed by reducing SDS-PAGE
Enzyme Activity ≥ 250 U/μL
Endotoxin Level ≤ 0.1 EU/kU as determined by gel clotting method.

  • Benz-Neburase™, Tag-free
  • Benz-Neburase™, Tag-free

    Lane M: DNA marker
    Lane 1: PCR product
    Lane 2: GenScript Benz-Neburase™, tag-free + PCR product
    Lane 3: Competitor endonuclease+ PCR product
    Lane 4: Genomic DNA
    Lane 5: GenScript Benz-Neburase™, tag-free + Genomic DNA
    Lane 6: Competitor endonuclease + Genomic DNA
    Lane 7: Plasmid DNA
    Lane 8: GenScript Benz-Neburase™, tag-free + Plasmid DNA
    Lane 9: Competitor endonuclease + Plasmid DNA
    Lane 10: RNA
    Lane 11: GenScript Benz-Neburase™, tag-free + RNA
    Lane 12: Competitor endonuclease + RNA

  • Benz-Neburase™, Tag-free
  • Benz-Neburase™, Tag-free

    Lane M:SDS-PAGE marker
    Lane R:Reducing (R)
    Lane N:Non-reducing (NR)
    Purity: > 95% as analyzed by SDS-PAGE


Target Background The Benz-Neburase is a genetically engineered endonuclease from Serratia marcescens used as a DNA eraser in the purification processes of biological molecules. The enzyme cleaves all forms of DNA and RNA into smaller nucleotides of around 5-8 base pairs. Benz-Neburase requires divalent cation, preferably Mg2+ for activity, displays a broad pH tolerance, ranging from pH 6 to pH 10, with an optimal pH of 8-8.5, and has a wide temperature tolerance, ranging from 35 °C to 44 °C. The nuclease is a physiologic homodimer and functions more progressively than the monomer. Two disulfide bonds in the nuclease are crucial to its activity and stability. The enzyme is active in a broad range of conditions and is free of proteolytic activity. This makes the enzyme especially useful for biopharmaceutical applications with contaminating DNA residue, such as lysed host cells in viral vector manufacturing processes.
Synonyms alternative to Benzonase®
Benzonase is a registered trademark of Merck KGaA
References 1. Nestle, Marion, and W. K. Roberts. "An extracellular nuclease from Serratia marcescens: I. Purification and some properties of the enzyme." Journal of Biological Chemistry 244.19 (1969): 5213-5218.
2. Benedik, Michael J., and Ulrich Strych. "Serratia marcescens and its extracellular nuclease." FEMS microbiology letters 165.1 (1998): 1-13.
3. Filimonova, Maria N., Kurt L. Krause, and Michael J. Benedik. "Kinetic studies of the Serratia marcescens extracellular nuclease isoforms." Biochemistry and molecular biology international 33.6 (1994): 122-1032.
4. Friedhoff, Peter, et al. "A procedure for renaturation and purification of the extracellular Serratia marcescens nuclease from genetically engineered Escherichia coli." Protein expression and purification 5.1 (1994): 37-43.
5. Franke, Ingo, Gregor Meiss, and Alfred Pingoud. "On the Advantage of Being a Dimer, a Case Study Using the Dimeric Serratia Nuclease and the Monomeric Nuclease from Anabaena sp. Strain PCC 7120." Journal of Biological Chemistry 274.2 (1999): 825-832.

For laboratory research use only. Direct human use, including taking orally and injection and clinical use are forbidden.


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