Our Mutant Proteinase K has higher specific activity and is more stable at room temperature compared with wild-type Proteinase K. It is a non-specific serine proteinase with broad substrates. It is active over the pH range from 4 to 12 and can be used in any situation to digest native and denatured proteins.
Our Mutant Proteinase K is included in New Products, Science Journal, March 8, 2019.
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Cat. No.: MPTK-10 (for 10g)
Cat. No.: MPTK-1000 (for 1kg)
Form: White Powder, Lyophilized from purified solids or liquid enzyme
Specific Activity: ≥30 U/mg dry weights
Package: 100 mg/bottle (Standard) or 1-200 gram custom packing.
Source: Pichia Pastoris with a mutant cloned gene from Tritirachium album limber
Molecular Weight: 29,300
Proteinase K dissolves in water at 1 mg/ml to give a clear colorless solution.
Store below 4°C.
Expiration: The expiration date is 3 years for powder and one year for liquid.
Dilution Buffer: 20 mM Tris-Cl (pH 7.4), 1 mM CaCl2, 50% glycerol.
Unit Definition: One unit is defined as the amount of enzyme that will liberate 1 µmol of tyrosine per minute from casein at 37°C at pH 7.5.
DNase Activity: None detectable after incubation with λ DNA for 6 hours at 37°C.
RNase Activity: None detectable after incubation with RNA for 16 hours at 25°C.
Protein Purity: Over 99% (Native-PAGE and SDS-PAGE assay)
The application of this Mutant Proteinase K is similar to wild-type Proteinase K. But this mutant one has higher specific activity and is more stable at room temperature. It is a non-specific serine proteinase with broad substrates. It is active over the pH range from 4 to 12. It can be used in any situation to digest native and denatured proteins. For instance, it is used for isolating mRNA or genomic DNA from different tissues and modifying glycoprotein for structure studies. Mutant Proteinase K is active with SDS, urea, and EDTA and active between 15°C and 75°C.
Kraus, E; et.al. Proteinase K from the Mold Tritirachium album limber, Specificity and Mode of Action. Z. Physiol. Chem., 357:939;1976.
Jany,KD, et al. Amino Acid Sequence of Proteinase K from the Mold, Tritirachium album limber. Proteinase K; a Subtilisin-related Enzyme with Disulfide Bonds. FEBS Letter, 199,139.1986.
Mutant Proteinase K is included in New Products, Science Journal, March 8, 2019. Please visit: