Recombinant Proteinase K, based on the enzyme from the fungus Tritirachium album Limber, is a serine protease that exhibits broad cleavage activity. It cleaves peptide bonds adjacent to the carboxylic group of aliphatic and aromatic amino acids and is useful for general digestion of protein in biological samples.
Recombinant expression of Proteinase K reduces risk of contamination, which when combined with our stringent quality system, ensures the high level of purity and consistency required by diagnostic and therapeutic developers.
The stability of Proteinase K in urea and SDS and its ability to digest native proteins make it useful for a variety of applications including preparation of chromosomal DNA for pulsed-field gel electrophoresis, protein fingerprinting and removal of nucleases from preparations of DNA and RNA. A typical working concentration for Proteinase K is 50–100μg/ml.
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