For research use only
Proteinase K is an active serine protease. It has nonspecific cleavage activity on a broad range of substrates including native and denatured proteins. Proteinase K is highly stable in the presence of denaturing agents, such as SDS and urea, and under a wide range of pH, temperature, and salt conditions. It is active between pH4 and 12, and between 0 and 75°C.
Proteinase K is widely used in the field of molecular biology. Its applications include, but are not limited to, digesting proteins in the preparation of DNA or RNA, digesting and thus inactivating enzymes including nucleases and phosphatases to terminate reactions, retrieving antigens from formalin-fixed, paraffin-embedded specimens for immunohistochemical staining, and adding to tail lysis buffer for genotyping purpose.
MW: 28.93 g/mol
Form: 20 mg/mL solution
Purity: >95% by native-PAGE
Source: Recombinant proteinase K from tritirachium album, produced in yeast
Grade: Molecular biology
Units/mg protein: >40
One unit liberates 1 µmol of tyrosine per minute from casein at pH7.5 at 37°C.
DNA/RNA: not detected
DNase: not detected
RNase: not detected
Endonuclease: not detected
Stable at -20°C for at least 1 year
Do not store in frost-free freezer