QIAGEN Protease (30 AU)

This broad-specificity serine protease from QIAGEN supports reliable DNA/RNA extraction and cell lysis workflows, cleaving preferentially at neutral and acidic residues. Isolated from a recombinant Bacillus strain, the enzyme offers broad substrate specificity in buffers commonly used in DNA and RNA extraction procedures and serves as an economical alternative endopeptidase for isolation of native DNA and RNA from a variety of biological samples.

QIAGEN Protease is particularly stable and active at high pH, delivering high specific activity in Tris-containing buffers of alkaline pH (7.5–10.5). Activity increases in the presence of strong denaturants such as urea and guanidine HCl, as well as with up to 1% SDS, and rises as a function of temperature (30–55°C). The enzyme is not inhibited by up to 100 mM EDTA in Tris-Cl buffers, although in the presence of greater than 1% SDS or other strong denaturants the EDTA concentration must be less than 8 mM. It is easily inactivated by incubation at 70°C for 15 minutes.

Classified as a serine-type protease containing a catalytic triad (Ser-His-Asp), this Bacillus-derived enzyme maintains stability under harsh conditions including high temperatures and in the presence of detergents and surfactants. QIAGEN Protease is completely free of DNase and RNase activities, making it an economical alternative for proteolysis during isolation of native DNA and RNA from a variety of sources. The protease is dedicated for use in various QIAGEN kits.