Description_x000D_ Application_x000D_ Proteinase K from Tritirachium album has been used:_x000D_ • in bovine endometrial epithelial cells for herpes viral DNA extraction_x000D_ • for viral RNA extraction from nasal swabs_x000D_ • as a component of phase lock and direct PCR lysis buffer_x000D_ The product has been used to study its pre-treatment effects on the silk fibroin. The aspects analysed in this study included the crystallographic properties of hydroxyapatite (HAp), and the microstructure and microhardness of the composites. The enzyme has also been used to facilitate the access of probes to rRNA using FISH techniques to detect pathogenic Staphylococcus aureus._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 has a broad specificity and degrades many proteins even in the native state. It mainly cleaves the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked α-amino groups. The molecular weight of proteinase K from amino acid sequence is found to be 28,930 Da and from SDS-PAGE, it is found to be 28,500 Da. The optimum pH is between 7.5-9.0 and its isoelectric point is 8.9. Ca2+ (1-5 mM) is required for its activation. Proteinase K is inhibited by DIFP (diisopropylfluorophosphate) or PMSF (phenylmethylsulfonyl fluoride)._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_ Physical form_x000D_ Solution in 40% glycerol (v/v) containing 10 mM Tris-HCl, pH 7.5, with 1 mM calcium acetate._x000D_ Legal Information_x000D_ PicoGreen is a registered trademark of Life Technologies