Proteinase K, Molecular Biology Grade
Proteinase K is a subtilisin-related serine protease that hydrolyzes a variety of peptide bonds and is frequently used to cleanup enzymatic reactions or cell lysates.
- Highly characterized for more consistent performance
- Optimal activity and stability for up to 24 months
- Active in a wide range of temperatures and buffers with optimal activity between 20 and 60°C and a pH between 7.5 and 12.0.
- No detectable endonuclease, exonuclease, DNase or RNase contaminating activities
Highly characterized for more consistent performance, Proteinase K is a subtilisin-related serine protease that will hydrolyze a variety of peptide bonds. Proteinase K is active in a wide range of temperatures and buffers with optimal activity between 20 and 60°C and a pH between 7.5 and 12.0 (1, 2). Activity is stimulated when up to 2% SDS or up to 4 M urea are included in the reaction (3). Calcium is important for thermostability of Proteinase K but it is not required for catalysis, therefore Proteinase K is also active in buffers containing chelating agents such as EDTA (4).
20 mg/ml, approximately, as determined by UV absorption at 280 nm.
Product SourceEngyodontium album (Tritirachium album)
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