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E8263

Sigma-Aldrich

Benzonase® Nuclease, ultrapure

≥250 units/μL, ≥99% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous glycerol solution, ultrapure grade

Synonym(s):

Endonuclease from Serratia marcescens

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Serratia marcescens

Quality Level

recombinant

expressed in E. coli

grade

ultrapure grade

Assay

≥99% (SDS-PAGE)

form

buffered aqueous glycerol solution

mol wt

30 kDa

concentration

≥250 units/μL

application(s)

research use

shipped in

wet ice

storage temp.

−20°C

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Application

The enzyme has been used for an assay to detect the amount of Tf1 RNA that is protected from degradation by the nuclease, Benzonase. The Tf1 element of Schizosaccharomyces pombe is a long terminal repeat-containing retrotransposon that encodes functional protease, reverse transcriptase, and integrase proteins. It has also been used in the fractionation of nuclear pellet and nuclear extract obtained from cell lysates.
Ultrapure benzonase nuclease, or Endonuclease from Serratia marcescens, has been used in a study to assess the effect of sodium dodecylbenzenesulfonate and antifoaming agents on the endonuclease activity of Serratia marcescens. Endonuclease from Serratia marcescens has also been used in a study to investigate the structure of chromatin subunits.
Used for the removal of nucleic acid from protein samples.

Biochem/physiol Actions

Benzonase® is a genetically engineered endonuclease from Serratia marcescens. The protein is a dimer of 30 kDa subunits with two essential disulfide bonds. 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. It completely digests nucleic acids to 5′- monophosphate terminated oligonucleotides 3 to 5 bases in length. This is ideal for the removal of nucleic acids from recombinant proteins. It can also be used 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 with this enzyme improves its resolution on 2D gel electrophoresis by eliminating any bound nucleic acids. The optimum pH for enzyme activity is found to be 8.0-9.2.
Digests native or heat-denatured DNA and RNA.

Unit Definition

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).

Physical form

Solution in 50% glycerol containing 20 mM Tris HCl, pH 8.0, 2 mM MgCl2, and 20 mM NaCl.

Legal Information

Benzonase® Nuclease is supplied by Merck KGaA, Darmstadt, Germany and/or its affiliates.
Benzonase is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Laure Teysset et al.
Journal of virology, 77(9), 5451-5463 (2003-04-15)
The Tf1 element of Schizosaccharomyces pombe is a long terminal repeat-containing retrotransposon that encodes functional protease, reverse transcriptase, and integrase proteins. Although these proteins are known to be necessary for protein processing, reverse transcription, and integration, respectively, the function of
Daria V Babushok et al.
Human mutation, 28(6), 527-539 (2007-02-20)
Long interspersed nucleotide element (LINE)-1 retrotransposon (L1) has emerged as the largest contributor to mammalian genome mass, responsible for over 35% of the human genome. Differences in the number and activity levels of L1s contribute to interindividual variation in humans
T K Ball et al.
Gene, 57(2-3), 183-192 (1987-01-01)
We are studying exoproteins of the enteric bacterium Serratia marcescens as a model system for the release of extracellular proteins from the cell. In this work we report the cloning of the gene for a secreted nuclease from S. marcescens
T K Ball et al.
Nucleic acids research, 20(19), 4971-4974 (1992-10-11)
The role of the two disulfide bonds found in the Serratia marcescens nuclease were tested by site directed mutagenesis and were found essential for nuclease activity, although slight residual activity remained. The requirement for disulfide bond formation may play a
Romain Da Costa et al.
Investigative ophthalmology & visual science, 57(13), 5326-5334 (2016-10-27)
Gene therapies to treat eye disorders have been extensively studied in the past 20 years. Frequently, adeno-associated viruses were applied to the subretinal or intravitreal space of the eye to transduce retinal cells with nucleotide sequences of therapeutic potential. In

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