Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA. Proteinase K is typically used at a concentration of 50-100 μg/ml. It is active with or without the presence of SDS, urea, EDTA or various metal ions, but the activity of proteinase K can be increased by adding the denaturing agents and the structure of proteinase K can be stabilized by addition of Ca 2+. Proteinase K is inactivated by heating to 95°C for 10 minutes or using an inhibitor such as PMSF, AEBSF or DFP. Product Specifications: Proteinase K, RNase/DNase free MOLECULAR BIOLOGY GRADE Molecular Weight: 28.5 kDa Activity: >= 30 U/mg Unit Definition: One unit is defined as the amount of enzyme that will liberate 1.0 μmol tyrosine (Folin-positive amino acid) from casein per minute at 37°C, pH 7.5. Storage / Handling: Store at -20°C. Reconstitute in 50mM Tris-HCl (pH 8.0), 3mM CaCl2.
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