Proteinase K, Recombinant, Molecular Biology Grade, 20 mg/mL SolutionProteinase K from Tritirachium album, expressed in Pichia pastoris, is a subtilisin related serine protease. It is a highly purifed and stable endopeptidase, widely used to remove DNases and Rnases during DNA RNA isolation. It remains stable and active in the presence of chemicals that usually denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. In the presence of