QIAGEN Protease and QIAGEN Proteinase K
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.
Proteinase K powder
Proteinase K powder is a lyophilized, white powder, highly
active with exceptional lot-to-lot consistency (see figure “High lot-to-lot
consistency Proteinase K powder”), ensuring reproducibility for stable working
conditions, repeatable and reliable experiment results. Proteinase K powder is
highly stable when stored at –20°C (see figure “Proteinase K powder
stability”).
Proteinase K powder specifications:
- No
detected exonuclease, endonuclease or RNase activity
- Solubility
in water ≥20 mg/mL; activity ≥30 U/mg lyophilizate; specific activity ≥40
U/mg protein; protein content ≥70%; DNA content ≤10 pg/mg
- Shipping
conditions: Ambient temperature
