PROTEINASE K CHROMATOGRAPHICALLY PURIFIE

Analysis Note

Appearance (color): whiteAppearance (description): lyophilisateActivity (hemoglobin; pH 7.5; 37 °C): ≥ 30.0 mAnsonU/mgSpec. activity (calc. on protein): ≥ 40 mAnsonU/mgDNases (Nicking activity; pBR 322; 6 h; 37 °C): not detectableRNases (RNA; 2 h; 37°C): not detectable

Application

Useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.Removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease A.Reported useful for the isolation of hepatic, yeast, and mung bean mitochondriaDetermination of enzyme localization on membranesTreatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling.Digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research.

Biochem/physiol Actions

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.

Packaging

100, 500 mg in Glass bottle