Benzonase Endonuclease

Description
Benzonase endonuclease from Serratia marcescens, can be used to degrade all forms of DNA and RNA while having no proteolytic activity. Benzonase endonuclease 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 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.

Features

Easy operation, time saving

Lower priced, cost-effective

No typical protease activity

Steady product quality

High purity, low pollution

Be used in more than 2000 proteins' purification

Suitable for recombinant antibody's purification

Suitable for vaccine's purification

Applications

Digest native or heat-denatured DNA and RNA.

Prepare proteins in microcalorimetric experiments.

Reduce cell clumping during the preparation of chimeric cell mixtures.

Preparation of nuclear extracts by digesting DNA and releasing nuclear proteins intimately associated with DNA.

Used for the removal of nucleic acid from protein samples.

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).

Purity
>95% determined by SDS-PAGE

Storage Conditions
50% Glycerol, 20 mM Tris HCl, pH 8.0, 2 mM MgCl2, 20 mM NaCl