DNA extraction Proteinase K solution 20mg/ml 1ml with CAS

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.

1.Useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.

2.Removal endotoxins bound to cationic proteins such as lysozyme and ribonuclease A.

3.Reported useful for the isolation of hepatic, yeast, and mung bean mitochondria

4.Determination of enzyme localization on membranes

Treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling.

5.Digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research.

 

100mg/bottle, 1ml/bottle, 10ml/bottle, when stored at –20 °C, the product retains activity for at least 1 years, ice bag transportation.