Digestion of proteins
Proteinase 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
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
Proteinase 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 Proteinase K inactivates DNases and RNases in eucaryotic and microbiological cell cultures. The use of Proteinase K during lysis of the cells allows the isolation of
intact highly-molecular nucleic acids.
Quality of Proteinase 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