Proteinase K is a stable serine protease with broad substrate specificity. Proteinase K 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. Proteinase K is commonly used for its broad specificity.
Benefits:
1. Higher stability and enzyme activity based on directed evolution technologies
2 Tolerant of Guanidine salt
3 Free of RNase DNase Nickase and heavy metal ions, DNA <5 pg/mg
4 Annual output of 1500 kg, the largest proteinase K supplier in China
Applications
Proteinase K can be used for genetic diagnostic kit; RNA and DNA extraction kits; Extraction of non-protein components from tissues, degradation of protein impurities, such as DNA vaccines and preparation of heparin; Preparation of chromosome DNA by pulsed electrophoresis; Western blot; Enzymatic glycosylated albumin reagents in vitro diagnosis.