Thermo Scientific Pierce Proteinase K is a protease that cleaves at the carboxyl side of aliphatic, aromatic or hydrophobic residues and is commonly used to digest and inactivate DNase and RNase during in nucleic acid purification.
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 Enzyme.
||Peptidase K, Tritirachium alkaline proteinase
||Cleaves at the carboxyl side of aliphatic, aromatic or hydrophobic residues
|Proteinase K Source
||>30 units/mg at 35°C
||RNase-free and DNase-free
||Inactivation of RNase and DNase during nucleic acid purification
||0.05-1 mg/ml proteinase K, pH 7.5-8, often containing 0.5-1% SDS
||Store at -20°C
||PMSF or DFP
- Ebeling, W., et al. (1974) Proteinase K from Tritirachium album limber. Eur. J. Biochem. 47,
- Liu, D., et al. (2003) Endocrinology. 144, 4894-4904.
Pierce Trypsin, MS Grade (Part No. 90057)
MS-Grade Proteases and Digestion Kits for Mass Spectrometry
Standard-Grade Proteases and Protease Resins
Enzymes for Cell Lysis