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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 |
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| 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 |
References
- Ebeling, W., et al. (1974) Proteinase K from Tritirachium album limber. Eur. J. Biochem.47,
91-97.
- Liu, D., et al. (2003) Endocrinology. 144, 4894-4904.
* Proteinase K and other proteases are available in bulk quantities for manufacturing applications.
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Certificate of Analysis
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