Synonym: Endonuclease from Serratia marcescens
|Related Categories||3.1.x.x Acting on esters, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Cell Lysis and Protein Extraction Reagents,|
|recombinant||expressed in E. coli|
|form||buffered aqueous glycerol solution|
|foreign activity||protease, essentially free|
Used for the removal of nucleic acid from protein samples.
Benzonase nuclease, or endonuclease from Serratia marcescens, can be used to degrade all forms of DNA and RNA while having no proteolytic activity. Benzonase nuclease can also be used to prepare proteins in microcalorimetric experiments.
The enzyme from Sigma has been used to limit cell clumping during the preparation of chimeric cell mixtures. It has also been used for the preparation of nuclear extracts by digesting DNA and releasing nuclear proteins intimately associated with DNA.
Digests native or heat-denatured DNA and RNA.
Benzonase® is a genetically engineered endonuclease from Serratia marcescens.1,2 The protein is a dimer of 30 kDa subunits with two essential disulfide bonds.3,4,5,6 This endonuclease attacks and degrades all forms of DNA and RNA (single stranded, double stranded, linear and circular) and is effective over a wide range of operating conditions. The optimum pH for enzyme activity is found to be 8.0-9.2. It completely digests nucleic acids to 5′- monophosphate terminated oligonucleotides 3 to 5 bases in length. This is ideal for removal of nucleic acids from recombinant proteins and for applications where complete digestion of nucleic acids is desirable. It also reduces viscosity in protein extracts and prevents cell clumping. Pre-treatment of a protein sample improves its resolution on 2D gel electrophoresis by eliminating any bound nucleic acids.
Benzonase® Nuclease is supplied by Merck KGaA and its affiliates.
Benzonase is a registered trademark of Merck KGaA
One unit will digest sonicated salmon sperm DNA to acid-soluble oligonucleotides equivalent to a ΔA260 of 1.0 in 30 min at pH 8.0 at 37 °C (reaction volume 2.625 ml).
Solution in 50% glycerol containing 20 mM Tris HCl, pH 8.0, 2 mM MgCl2, and 20 mM NaCl.
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≥250 units/μL, ≥99% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous glycerol solution, ultrapure grade
For bacterial cell lysis, standard strength
For bacterial lysis
lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein
used for cell and subcellular organelle isolation
The field of proteomics is continually looking for new ways to investigate protein dynamics within complex biological samples. Recently, many researchers have begun to use RNA interference (RNAi) as ...
LSI Issue 24
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4. A procedure for renaturation and purification of the extracellular Serratia marcescens nuclease from genetically engineered Escherichia coli. Friedhoff P, Gimadutdinow O, Rüter T, et al. Protein Expr. Purif. 5(1), 37-43, (1994)
Production and comprehensive quality control of recombinant human Interleukin-1beta: a case study for a process development strategy. Block H, Kubicek J, Labahn J, et al. Protein Expr. Purif. 57(2), 244-54, (2008)
Quantitative determination of the infectivity of the proviral DNA of a retrovirus in vitro: Evaluation of methods for DNA inactivation. Sheng-Fowler L, Lewis AM, and Peden K Biologicals 37(4), 259-69, (2009)
Post-ischemic administration of peptide with apurinic/apyrimidinic endonuclease activity inhibits induction of cell death after focal cerebral ischemia/reperfusion in mice. Kim HW, Cho KJ, Lee BI, et al. Neurosci. Lett. 460(2), 166-9, (2009)
Polymerase chain reaction, nuclease digestion, and mass spectrometry based assay for the trinucleotide repeat status of the fragile X mental retardation 1 gene. Dodds ED, Tassone F, Hagerman PJ, et al. Anal. Chem. 81(13), 5533-40, (2009)
A simple and effective method to generate lentiviral vectors for ex vivo gene delivery to mature human peripheral blood lymphocytes. Yang S, Karne NK, Goff SL, et al. Hum. Gene Ther. Methods 23(2), 73-83, (2012)
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of chlorite dismutase: a detoxifying enzyme producing molecular oxygen. de Geus DC, Thomassen EA, van der Feltz CL, et al. Acta Crystallogr. F, Struct. Biol. Cryst. Commun. 64(Pt 8), 730-2, (2008)
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