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Proteinase K (EC 3.4.21.64) is an extracellular serine endopeptidase initially discovered from fungus Tritirachium album Limber. Proteinase K belongs to the peptidase family S8, and its predominant cleavage site is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked α-amino groups [1] [2]. Because of its broad sequence specificity and stability in variant pH and temperature conditions, proteinase k is commonly used in biology sample processing. Proteinase K is stable over a wide pH range from 4-12, when pH is 8.0 [3], the activity reaches the peak, the activity also increases with elevated temperature from 37oC to 60oC. Some denature reagents extensively used in nucleic acid purification don%› inhibit proteinase K%š activity, such as 3M Guanidinium Chloride, 3M Guanidinium Thiocyanate, 1% SDS and 4M urea etc, which make proteinase K a favorite tool by molecular biologist in protecting RNA or DNA from degradation by nucleases, for example, proteinase K can be added to extraction buffer during nucleic acid preparation to cleave nucleases such as DNases and RNases, and preserve the nucleic acids from degradation.

For the time being COVID-19 pandemic is threatening human life, and has been causing huge damage globally, COVID-19 RNA identification by PCR is the golden standard for diagnosis, virus sample preparation is a key step in the diagnosis procedure, proteinase K is one of the important reagent to make sure that the target RNA is intact during the sample preservation and processing [4]. AmeriDx Proteinase K has high purity (>98%) and great activity (>=30U/mg), and meet your requirement for virus detection.