Description
Proteinase K is 28.9 kDA serine protease produced by a recombinant strain of Pichia pastoris bearing the proteinase K gene of the fungus Tritirachium album. The enzyme has a broad substrate specificity for a large number of proteins. It hydrolyses the polypeptide chain mainly at sites containing nonpolar amino acids. The reagent can be used for hydrolysis of proteins during the isolation and purification of nucleic acids.
Enzyme possesses high purity and decreased amount of host DNA recombinant enzyme for no cross-reactivity contamination in NGS or molecular diagnostic applications. Proteinase K stable at wide range of pH (4.0–12.5) and at elevated temperatures (up to 56 °C).