Omni-nuclease (Benzonase)

The Omni-nuclease is the nuclease from Serratia marcescens , also known as Benzonase, obtained through yeast recombinant expression. This enzyme is composed of two subunits, each with a size of 26 kDa. Its activity is 34 times stronger than that of DNase I, efficiently hydrolyzing various forms of DNA and RNA to 5'-monophosphate oligonucleotides with lengths of 3 to 5 bases. The enzyme's activity requires Mg2+, with an optimal pH range of 6 to 10 and an ideal reaction temperature of 37°C . This product is free from bacterial endotoxin residues and maintains high stability and activity under a wide range of conditions, such as 6 M urea, 0.1 M Guanidine HCl, 0.4% Triton X100, 0.1% SDS, 1 mM EDTA, 1 mM PMSF, or 0.4% Sodium deoxycholate. It is highly suitable for the vaccine, protein, and polysaccharide pharmaceutical industries, removing nucleic acid residues from samples or products, thereby enhancing sample purity and the biological efficacy of the products.