Proteinase K is a highly active serine protease with broad cleavage specificity on native and denatured proteins.
Proteinase K is widely used in the purification of native RNA and DNA from tissues or cell lines, as well as for many other applications.
• High activity – broad-spectrum serine protease
• Active under denaturing conditions – useful for a variety of applications
• Stable – at high temperatures
• Molecular biology grade – useful for general digestion of proteins
• Proteinase K is also available as a stabilized stock solution
Proteinase K is a highly active serine protease (MW 28,500 Da) isolated from the fungus Tritirachium album. The enzyme exhibits broad cleavage specificity on native and denatured proteins and is widely used in the purification of native RNA and DNA from tissues or cell lines. Because the solution is tested for the absence of RNases and DNases, it is ideal for isolating PCR and RT-PCR templates.
The activity of Proteinase K is increased in the presence of denaturants such as SDS (1%) and elevated temperature (50-60°C). The recommended working concentration is 50-100 μg/mL for protein removal and enzyme inactivation and up to 2 mg/mL for tissue treatment.
Proteinase K products are free of detectable DNase and RNase.
SKU: | Size: | Webshop: |
BIO-37037 | 100 mg | Orde online |
BIO-37039 | 1000 mg | Orde online |
All components should be stored at -20°C upon receipt for optimum stability. Repeated freeze/thaw cycles should be avoided.
When stored under the recommended conditions and handled correctly, full activity of the reagents is retained until the expiry date indicated on the outer box label.
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