Proteinase K is a powerful proteolytic enzyme isolated from Candida albicans. It has high specific activity and is a key reagent for DNA extraction. 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 a stable and highly reactive serine protease. It cleaves the carboxy terminal peptide bonds of aliphatic amino acids and aromatic amino acids. This enzyme has been purified to remove the activities of RNase and DNase. Because proteinase K is stable in urea and SDS and has the ability to degrade natural proteins, therefore it has a wide range of applications, commonly used in molecular biology, cell biology, immunohistochemistry and other related experiments to digest various proteins, including preparation of chromosomal DNA for pulse electrophoresis, western blotting, and removal of nucleases in DNA and RNA preparation.
When stored at –20 °C, the product retains activity for at least 1 years, ice bag transportation.
Can be used in conjunction with our company's TUNEL kit:
Dilute 10 times with PBS (pH 7.4) before usage to prepare proteinase K working solution. Take a certain amount of working solution to cover the tissue, and incubate at 37°C for 10~30 min. Then wash the slides three times with PBS (pH 7.4) in shaker, 5 min each time.
1. It is recommended to use in separate package, avoid repeated freezing and thawing.
2. Due to the high activity and stability of the proteinase K, cross-contamination in the experiment should be avoided.
3. For your safety and health, please wear lab coats and disposable gloves.