Proteinase K is a subtilisin-like endolytic protease that is isolated from the saprophytic fungus Tritirachium album. It has a high activity that is stable across a wide range of pH and temperature conditions and is suited to short digestion times. The activity of proteinase K is increased at elevated temperatures up to 65°C. Calcium is not essential to the function of proteinase K. Therefore, EDTA and other chelating agents do not interfere with the activity and may be used alongside proteinase K to inactivate calcium-dependent nucleases in DNA and RNA preparation. | Properties of Proteinase K | | | Alternate names | Peptidase K, Tritirachium alkaline proteinase | | Specificity | Cleaves at the carboxyl side of aliphatic, aromatic or hydrophobic residues | | Proteinase K Source | Tritirachium album | | Molecular weight | 28,900 | | Form | Lyophilized form | | Concentration/activity | >30 units/mg at 35°C | | RNase/DNase | RNase-free and DNase-free | | Protease type | Serine protease | | Uses/applications | Inactivation of RNase and DNase during nucleic acid purification | | Reaction conditions | 0.05-1 mg/ml proteinase K, pH 7.5-8, often containing 0.5-1% SDS | | Storage conditions | Store at -20°C | | Inhibitors | PMSF or DFP |
Product # | Description | Pkg. Size | 17916 | Proteinase K
Proteinase K, from tritirachium album | 100 mg |
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