Description

• 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.[1]
• Application: Turbonuclease from Serratia marcescens has been used for cell lysis during proximity biotinylation assay (BioID) and affinity-purification[2]. It has also been used as a component of lysis buffer for protein extraction from cell lines for affinity purification studies.[3]
• 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.[1]
• 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