Benzonase Nuclease/NucA

NucA or Benzonase nuclease was first identified from Serratia marcesens, a gram-negative bacteria that lives naturally in soil and aquatic environments. Benzonase is a non-specific nuclease with high activity and specificity; it degrades both single- and double- stranded DNA and RNA. Benzonase belongs to a large class of magnesium dependent nucleases that are found throughout nature. The active protein is a homodimer of two 30 kDa subunits containing two disulfide bonds that are essential for activity and stability. This endonuclease attacks and degrades all forms of nucleic acids (single- and double-stranded, linear and circular) and is active over a range of operating conditions. The optimum pH range for enzyme activity of Benzonase is 8.0-9.2. It hydrolyzes internal phosphodiester bonds between nucleotides in nucleic acids to produce 5'-monophosphate oligonucleotides of 3-8 bases in length. Benzonase is ideal during protein purification and other applications where removal of contaminating nucleic acids is desired. It is also effective at reducing viscosity of cell lysates and limiting cell aggregation and clumping.