innuPREP - Proteinase K
Proteinase K is one of the most active endopeptidases known. The enzyme is extraordinarily effective against native proteins and can be used for quickly inactivating endogenous RNases and DNases. Proteinase K is particularly suitable for isolating nucleic acids for use in amplification reactions, for isolating native RNA and DNA from tissues and cell lines, for promoting cell lysis by activating a bacterial autolysis factor, and for modifying proteins and/or glycoproteins on cell surfaces (for membrane structure analyses).
Highly active recombinant protease from Pichia pastoris with endo- and exoproteolytic activity
- Inhibitors: None of the following inactivate the enzyme: metal ions, chelating agents (such as EDTA), sulfhydryl reagents, or trypsin and chymotrypsin inhibitors.
- Activators: Proteinase K activity is stimulated by the presence of denaturing agents (SDS and urea).
- Note: SDS can produce a seven-fold increase in Proteinase K activity.
- Optimum pH: Proteinase K is stable over a broad pH range (4 to 12.5), and retains its full activity for several hours if incubated at a pH between 6.5 and 9.5.
The enzyme can reduce proteins to free amino acids if a large excess of protein is present and if incubated for long periods of time.
- Contains no RNases or DNases, and virtually no DNA
- Consistent quality and performance
- Robust enzyme: stable over a broad pH range
- Ideal for a diverse array of applications, such as preparing cell lysates for subsequent nucleic acid isolation
20 mg/mL at an activity of 20 U/mg
Proteinase K is lyophilized and purified via chromatography, after which it is tested to ensure that no RNases, DNases and exonucleases are present. These should not be detectable.