Everything about Proteinase K totally explained
Proteinase K (also
protease K or
endopeptidase K) is a broad-spectrum
serine protease. The enzyme was discovered in 1974 in extracts of the
fungus Tritirachium album.
Proteinase K is commonly used in
molecular biology to digest protein and remove contamination from preparations of
nucleic acid. Addition of proteinase K to nucleic acid preparations rapidly inactivates
nucleases that might otherwise degrade the DNA or RNA during purification. It is highly-suited to this application since the enzyme is active in the presence of chemicals that
denature proteins, such as
SDS and
urea, chelating agents such as
EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is also stable over a wide pH range (4-12), with a pH optimum of pH 7.5-12.
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