Description_x000D_ Application_x000D_ Useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA._x000D_ Removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease A._x000D_ Reported useful for the isolation of hepatic, yeast, and mung bean mitochondria_x000D_ Determination of enzyme localization on membranes_x000D_ Treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling._x000D_ Digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research._x000D_ Biochem/physiol Actions_x000D_ Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA._x000D_ Unit Definition_x000D_ One unit will hydrolyze urea-denatured hemoglobin to produce color equivalent to 1.0 μmole of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent)._x000D_ Legal Information_x000D_ PicoGreen is a registered trademark of Life Technologies