Proteinase K is a non-specific protease of the serine protease family that cleaves peptide bonds adjacent to the carboxylic group of aromatic and aliphatic amino acids. Proteinase K is commonly used to digest proteins in biological samples, remove endogenous nucleases during DNA and RNA purification, unmask antigens in immunochemistry, and prepare tissues for in situ hybridization.
Proteinase K is active under a wide range of pH (between 6.5 and 9.5), elevated temperatures, and the presence of metal chelating agents and SDS.
A typical working concentration for Proteinase K is 50–100 μg/mL.
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