QIAGEN Protease and QIAGEN Proteinase K offer broad substrate specificity with high activity for a wide range of reaction conditions. Both proteases offer high activity in buffers commonly used in most DNA and RNA isolation procedures and are quality-guaranteed by QIAGEN.
Performance
QIAGEN Protease and QIAGEN Proteinase K offer broad substrate specificity with high activity in buffers commonly used in most DNA and RNA isolation procedures. Both enzymes are quality-guaranteed by QIAGEN. QIAGEN Protease is particularly stable and active at high pH. In Tris-containing buffers of alkaline pH (7.5 - 10.5) QIAGEN Protease displays 30 to 40% higher specific activity than Proteinase K. The enzyme can be easily inactivated by incubation at 70°C for 15 minutes.
In the presence of strong denaturants, such as urea (0.75 - 3 M urea) or guanidine HCl (0.5 - 3.0 GuHCl), the specific activity is comparable to that of Proteinase K, provided the EDTA concentration is less than 8 mM.
QIAGEN Protease shows increased activity in the presence of urea and guanidine HCl. Similar stimulation is obtained upon the addition of up to 1% SDS. Enzymatic activity also increases as a function of
temperature (30-55°C). For more detailed information, refer to the QIAGEN Protease Product Sheet in the Resources section.
QIAGEN Protease is not inhibited by up to 100 mM EDTA in Tris·Cl buffers. However, in the presence of greater than 1% SDS or other strong denaturants, the EDTA concentration must be less than 8 mM.
For protease digestion in DNA and RNA isolation procedures
Fully compatible with selected QIAGEN protocols
Both enzymes quality-guaranteed by QIAGEN
QIAGEN Protease and QIAGEN Proteinase K provide protease digestion during DNA and RNA preparation. Subtle differences between the enzymes should be considered when planning protease digestions.
