Proteinase K is a non-specific endoproteinase, which is a serine protease that can cleave ester bonds and peptide bonds connected to the carboxyl ends of aliphatic amino acids, hydrophobic amino acids and aromatic amino acids.
Recombinant Proteinase K is a non-specific endoproteinase, which is a serine protease that can cleave ester bonds and peptide bonds connected to the carboxyl ends of aliphatic amino acids, hydrophobic amino acids and aromatic amino acids. The molecular weight is 28.9 kDa (monomer). It is active at pH 4 to pH 12. It is also stable in the presence of SDS, urea or EDTA. It can cleave the carboxy terminal peptide bonds of aliphatic and aromatic amino acids, and is used for the degradation of proteins in biological samples. This enzyme has been decolorized and purified by chromatography to remove RNA and DNA, and the activity of other miscellaneous enzymes can not be detected. Because proteinase K is stable in urea and SDS, and has the ability to degrade natural proteins, the smallest polypeptide that is hydrolyzed is a tetrapeptide molecule.
High purity: no other miscellaneous enzyme activity: no other side reactions in the digestion reaction, high yield
Source: Tritirachium album limber
Molecular weight: 28.9kDA
Activity： Definition of activity unit: Under the conditions of 37°C and pH 7.5, the amount of proteinase K that can hydrolyze the substrate casein to produce 1 μmol of tyrosine per minute is defined as one unit (U).
Storage： The dry powder state can be stored at a low temperature under the condition of 0~4℃. After dissolving, divide into proper volume and store at -20℃.
Stability： Transportation can be carried out at room temperature.
Product name: Recombinant Proteinase K
Specific activity: ≥30 u/mg pro
Packaging: 100mg, 1g, >25g tube or bottle or bag etc
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