Merck
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E1014

Millipore

Benzonase® Nuclease

≥250 units/μL, ≥90% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous glycerol solution

Synonym(s):
Endonuclease from Serratia marcescens
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.54

Quality Level

recombinant

expressed in E. coli

assay

≥90% (SDS-PAGE)

form

buffered aqueous glycerol solution

mol wt

30 kDa

concentration

≥250 units/μL

foreign activity

protease, essentially free

shipped in

wet ice

storage temp.

−20°C

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Application

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.
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.
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. 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.
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

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

Enter Lot Number to search for Certificate of Origin (COO).

More Documents

Quotes and Ordering

Jos J M Drabbels et al.
Blood, 118(19), e149-e155 (2011-09-21)
Microchimerism is defined by the presence of low levels of nonhost cells in a person. We developed a reliable method for separating viable microchimeric cells from the host environment. For flow cytometric cell sorting, HLA antigens were targeted with human
Janus S Jakobsen et al.
Science advances, 5(7), eaaw4304-eaaw4304 (2019-07-17)
The key myeloid transcription factor (TF), CEBPA, is frequently mutated in acute myeloid leukemia (AML), but the direct molecular effects of this leukemic driver mutation remain elusive. To investigate CEBPA mutant AML, we performed microscale, in vivo chromatin immunoprecipitation sequencing
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
P Friedhoff et al.
Protein expression and purification, 5(1), 37-43 (1994-02-01)
Overproduction of the extracellular Serratia marcescens nuclease in Escherichia coli results in aggregation and sequestration of a large amount of the protein in inclusion bodies. Only a relatively small amount is secreted into the medium from which it can be
G N Eaves et al.
Journal of bacteriology, 85(2), 273-278 (1963-02-01)
Eaves, George N. (Wayne State University College of Medicine, Detroit, Mich.) and Charles D. Jeffries. Isolation and properties of an exocellular nuclease of Serratia marcescens. J. Bacteriol. 85:273-278. 1963.-The exocellular nuclease of Serratia marcescens, isolated by anion-exchange chromatography on diethylaminoethyl-Sephadex

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