QIAGEN Protease (30 AU)，19157，Qiagen，凯杰

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. 
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.

The enzyme can be easily inactivated by incubation at 70°C for 15 minutes.
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.