Enzyme for 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 (haemoglobin, 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 haemoglobin as 1 μmol
The protease or - its solution 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 inactivates DNases and RNases in eukaryotic and microbiological cell cultures. The use of Proteinase K during lysis of the cells allows the isolation of
intact highly-molecular nucleic acids.
- purified by chromatography and lyophilised
- RNases: not detectable
- DNases: not detectable
- Exonucleases: not detectable
Each batch of Proteinase K is tested for the presence of fungal and bacterial DNA. Moreover, the specific activity assay of each
batch of the enzyme is performed.
4 °C or -20 °C for at least 24 months, shipment at ambient temperature
Storage buffer: As an option GeneON offers: 50 mM Tris HCl (pH 8.0), 1 mM CaCl2, 50 % Glycerin (other buffers or other concentrations on request)
Determination of the the stability of Proteinase K during long-term storage at room temperature. The tested Lot was compared to the fresh production batch in 6 month time intervals. Assay
conditions described below.
Lot: tested: P040917 control LOT: current production batch
Storage buffer for Proteinase K in solution:
20 mM Tris pH 7,5, 1 mM CaCl2, 0,02% sodium acid, 50% glycerol (v/v).