Proteinase K isolated from Tritirachium album is used for protease digestion during DNA and RNA preparation. It is a serine protease that exhibits broad cleavage specificity. With a molecular weight 28.900 kD, it cleaves peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids.
It is not inactivated by chelating reagents such as EDTA or detergents such as SDS and is active over a wide range of pH (4-12.5).
Highly active and stable: > 30 units/mg protein (hemoglobin, pH 7.5, 37 °C).
High Quality: free of RNases, DNases and Exonucleases contamination.
Purified by chromatography.
Low cutting specificity.
Risk-free: product covered by our Quality 100% Guarantee.