Details
Proteinase K is an endolytic protease that cleaves peptide bonds at the carboxylic sides of aliphatic, aromatic or hydrophobic amino acids. Proteinase K is classified as a serine protease. The smallest peptide to be hydrolysed is a tetrapeptide.
Other applications: Proteinase K digests native proteins very effectively. It can therefore be used to remove 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