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Turbonuclease from Serratia marcescens

recombinant, expressed in E. coli

Endonuclease from Serratia marcescens
CAS Number:
Enzyme Commission number:
MDL number:


expressed in E. coli

Quality Level




≥200,000 units/mL

storage temp.


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General description

Endonuclease from Serratia marcescens is a dimer containing two identical monomeric units with distinct protein folds. The core contains a six-stranded antiparallel β-sheet flanked by α-helices on either side. Each monomer bears one active site. This enzyme is a magnesium-dependent nucleases.


Turbonuclease from Serratia marcescens has been used for cell lysis during proximity biotinylation assay (BioID) and affinity-purification. It has also been used as a component of lysis buffer for protein extraction from cell lines for affinity purification studies.
Turbonuclease has been used in a study to assess the TY3 gag3 spacer effect on intracellular condensation and uncoating.
Used for the removal of nucleic acid from protein samples.

Biochem/physiol Actions

Endonuclease from Serratia marcescens is effective against both single- and double-stranded DNA and RNA. It mediates the digestion of the 3′ O—P bond resulting in oligonucleotides ending with 5′ monophosphate. The activity of this enzyme is known to be less affected by the reducing and chaotropic agents. It is highly stable at room temperature. This endonuclease eliminates the undesired nucleic acids in downstream processing.
Turbonuclease provides a nuclease treatment by reducing viscosity and degrading RNA, genomic DNA, baculovirus DNA, and unencapsidated vector DNA.
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.

Physical form

Supplied as a solution in 50 mM Tris-HCl, pH 8.0 and 50 mM NaCl

Storage Class Code

12 - Non Combustible Liquids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

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Certificate of Origin

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