– Digestion of proteins
Proteinasa K is a serine protease that exhibits a very broad cleavage specificity. The Protein with a molecular weight 28.900 kD cleaves peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids. Proteinase K 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).
Activity: > 30 units/mg protein (hemoglobin, pH 7.5, 37°C)
Unit definition One unit is the amount of enzyme which releases at 37°C in 1 min as many folin-positive amino acids and peptides from hemoglobin as 1 μmol of tyrosine.
Proteinase K is a highly active and stable protease with low cutting specificity. The enzyme belongs to the group of subtilisine-related serine proteases and is
strongly inhibited by PMSF.
In presence of 0.5 – 1 % SDS Proteinasa K inactivates DNases and RNases in eucaryotic and microbiological cell cultures. The use of Proteinasa K during lysis of the cells allows the isolation of intact highly-molecular nucleic acids.
Quality Proteinasa K:
– purified by chromatography and lyophilised
– RNases: not detectable
– DNases: not detectable
– Exonucleases: not detectable
4 °C or -20 °C for at least 24 months, shipment at ambient temperature