Proteinase K - Solid

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.