Proteinase K （39450-01-6）Is The Most Active of The Existing Proteases

Proteinase K is a serine protease that was first discovered in extracts of Tritirachium album limber in 1974 . Since the enzyme is capable of digesting the natural keratin rich in disulfide bonds, Candida albicans can grow with keratin as the sole carbon source/nitrogen source, and the proteinase K is also named. Proteinase K is the superior product of Yacoo Science and Technology. Its CAS number is 39450-01-6 and the article number is D0002. Proteinase K is a serine protease with broad cleavage activity and is considered to be the most active of the existing proteases.

The biggest feature of proteinase K is its broad-spectrum and efficient cutting ability for natural proteins, which is the most active of the existing proteases. The enzyme prefers to cleave fatty amino acids and aromatic amino acids, particularly the carboxy terminal peptide bonds of alanine.

Proteinase K is an excellent enzyme with activity at pH 4~pH 12, 20°C~60°C, and a variety of chemical reagents (such as SDS, urea, and chelate) that can denature proteins. Mixtures (such as EDTA) and sulfhydryl reagents (such as trypsin inhibitors or chymotrypsin inhibitors) also have the ability to cleave proteins.

In summary, compared with other proteases, proteinase K has high activity and high stability. Its enzyme activity will not be inhibited by denaturants such as urea, SDS and EDTA, nor will it change due to high temperature, high salt or high pH, that is, proteinase K under high temperature, high salt or high pH and other conditions Can still maintain a higher activity.

Therefore, proteinase K is widely used in biochemical experiments and is a key reagent for DNA extraction. In addition, proteinase K is also widely used in leather, fur, silk, medicine, food, brewing and other aspects.

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