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Proteinase K is an endoproteolytic enzyme that cleaves peptide bonds at the carboxylic sides of aliphatic, aromatic or hydrophobic amino acids. Proteinase K is classified as a nonspecific serine protease. The smallest peptide to be hydrolysed is a tetrapeptide.
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Applications: Proteinase K effectively digests native proteins. It can be used to inactivate DNases and RNases when isolating DNA and RNA from tissues or cells.
Usage Conditions:
• Proteinase K is active over a wide pH range—optimal activity between 6.5 and 9.5
• Under denaturing conditions—e.g., in the presence of SDS or urea
• In the presence of metal chelating agents—e.g., EDTA
• At high temperatures—optimum digestion temperature is 65°C
Unit Definition: One unit of the enzyme liberates folin-positive amino acids and peptides corresponding to 1μmol tyrosine in 1min at 37°C using denatured hemoglobin as substrate.
Quality Control: Tested for the absence of endo-, exodeoxyribonucleases and ribonucleases
