Proteinase K (100mg)

Proteinase K, originally isolated from the mold Tritirachium album, is a serine protease with broad substrate specificity and relatively high proteolytic activity. It preferentially cleaves ester and peptide bonds adjacent to the C-termini of hydrophobic, aliphatic, or aromatic amino acids. CUSABIO’s recombinant proteinase K is highly pure determined by SDS-PAGE and reached up to 95%. It is characterized by high purity, sterility, no bio-burden, and no presence of DNAse, RNAse, DNA, and RNA contaminants. Its enzyme activity was calculated >30U/mg using the absorbance A275 as the vertical axis and different concentrations of a tyrosine as the horizontal axis. The working concentration of proteinase K, usually determined by the temperature, PH, and whether the buffer used contains SDS and urea, is 20mg/mL. This recombinant proteinase K protein is in-stock now. Proteinase K has a wide range of applications. In nucleic acid extraction and isolation, proteinase K can be used to degrade D…Read more