from Tritirachium album
For in vitro use only!
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 of tyrosine.
Shipping: shipped on blue ice
Storage Conditions: store at -20 °C
avoid freeze/thaw cycles
Shelf Life: 12 months
Molecular Weight: 28.9 kDa
EC number: 254-457-8
Purity: free of RNases, DNases and Exonucleases
Specific activity: > 30 units/mg
DNase activity: not detectable
RNase activity: not detectable
Digestion of proteins during DNA and RNA preparation.
Proteinase K is a serine protease that exhibits a very broad cleavage specificity. The protein with a molecular weight of 28.9 kDa cleaves peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids. Proteinse K is not inactivated by metal chelating reagents such as EDTA or detergents such as SDS and is active over a wide range of pH (4 - 12.5).
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 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.