Benz-Neburase™, His
This enzyme can be used to remove all forms of DNA and RNA, including double stranded, single stranded, linearized, and circular forms.
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| Z03626-10 | |
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| ￥312 | |
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| Expression System | E.coli |
| Tag | N-terminal 6× His Tag |
| Species | Serratia Marcescen |
| Biological Activity | ≥ 1.1×106 U/mg |
| Enzyme Activity | ≥ 250 U/μL |
| Unit Definition | One unit of Benz-Neburase™, His is defined as the amount of enzyme that causes a ∆A260 of 1.0 (equivalent to the complete digestion of 37μg DNA) in 30 min. |
| Purity | ≥ 95% as analyzed by reducing SDS-PAGE |
| Endotoxin Level | ≤ 0.1 EU/kU as determined by gel clotting method |
| Theoretical Molecular Weight | 27.5 kDa |
| Apparent Molecular Weight | ~27.5 kDa, on SDS-PAGE under reducing conditions |
| Formulation | Supplied as a solution of 20 mM Tris-HCl, 2 mM MgCl2, 20 mM NaCl, 50% Glycerol, pH 8.0. |
| Application |
This enzyme can be used to remove all forms of DNA and RNA,
including double stranded, single stranded, linearized, and circular
forms. Notes: The activity of Benz-Neburase™, His requires 1-2 mM Mg2+. |
| Storage & Stability | This product remains stable for 2 weeks at 4 °C or 24 months at - 20 °C. Avoid repeated freeze-thaw cycles. Do not store below -20 °C! |
Lane M：DNA marker
Lane 1：GenScript Benz-Neburase™, His + PCR product
Lane 2：PCR product
Lane 3：GenScript Benz-Neburase™, His + Genomic DNA
Lane 4：Genomic DNA
Lane 5：GenScript Benz-Neburase™, His + Plasmid DNA
Lane 6：Plasmid DNA
Lane 7：GenScript Benz-Neburase™, His + RNA
Lane 8：RNA
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Lane M：SDS-PAGE marker
Lane 1：Reducing ( R)
Lane 2：Non-reducing (NR)
Purity: > 95% as analyzed by SDS-PAGE
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| Synonyms |
alternative to Benzonase® Benzonase is a registered trademark of Merck KGaA |
| 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 pH10, optimal at 8-8.5, and has a wide temperature tolerance, ranging from 35℃ to 44℃. 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 applications with challenging DNA contents such as lysed host cells in viral vector manufacturing processes. |
| 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 research use only. Not intended for human or animal clinical trials, therapeutic or diagnostic use.
