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WHAT IS PROTEINASE K MADE OF? Proteinase K is known enzyme belonging to the class of serine proteases that cleave adjacent to the carboxylic group peptide bonds of aromatic and aliphatic amino acids. It's also exhibited a very broad cleavage specificity. The enzyme was discovered in extracts of the fungus Engyodontium album. HOW DOES PROTEINASE K WORK? In molecular biology, main application of proteinase K is to digest proteins during nucleic acids purification in order to remove protein contaminants: - Proteinase K quickly inactivates nucleases (enzymes that digest nucleic acids) that degrade DNA or RNA molecules during the cleansing. - Proteinase K is activated by calcium. It does not affect the activity of the proteinase, but protects again autolysis, improves thermal stability, and regulates substrate binding capacity. To increase the stability of Proteinase K, thereby enhancing its action, Urea as well as SDS (sodium dodecyl sulfate) or elevated temperature at 37-60C is commonly used. Inactivation of Proteinase K is occurring at temperature above 65C. WHAT IS THE PURPOSE OF PROTEINASES? Proteinase K is used to break down proteins in cell lysates (tissues, cell culture cells) and to release nucleic acids due to its action described above. Proteinase K application purpose: DNA isolation from various tissues; Removal of DNAses and RNAses: Proteinase K and RNases can act together in the lysis buffer to degrades contaminating RNAs and proteins;