Proteinase K (liquid)

Proteinase K is a stable serine protease with broad substrate specificity. It degrades many proteins in the native state even in the presence of detergents. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active site catalytic triad (Asp39-His69-Ser224). The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups. It is commonly used for its broad specificity.

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