innuPREP Proteinase K
Features
- Highly active recombinant protease from Pichia pastoris with endo- and exoproteolytic activity
- 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
Product Info
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).
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.
Order Info
Order numer | Quantity |
|---|---|
845-CH-0010006 | 6.0 mg (add 0.3 mL ddH2O) |
845-CH-0010030 | 30.0 mg (add 1.5 mL ddH2O) |
Specifications
Concentration:
20 mg/mL at an activity of 20 U/mg
Quality control:
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.
Downloads
- Manual innuPREP Proteinase K .pdf | 379.08 kB
(e.g. Manual, Short Manual)
