Recombinant Proteinase K
July 19, 2018
Creative Enzymes provides molecular biology grade lyophilized powder of Recombinant Proteinase K with various package sizes. Our product has high specific activity, superior purity, and outstanding stability in a wide range of pH and temperature. Inquiry online.
Proteinase K is a broad-spectrum serine protease originally isolated from fungus Engyodontium album (Tritirachium album). The enzyme was named “proteinase K” for its ability to digest keratin. Structural and molecular biology studies suggest that the enzyme belongs to the subtilisin family characterized with a catalytic triad (Asp39-His69-Ser224) in the active site. Proteinase K has no pronounced cleavage specificity and the preferential cleavage site is the peptide bond adjacent to hydrophobic amino acids.
Advantages of Our Recombinant Proteinase K
- Our recombinant proteinase K is a mutant of the native proteinase that obtained improved specific activity, higher efficiency and a wider range of pH and temperature while retaining optimal activity.
- The board temperature profile of our recombinant proteinase K helps with protein unfolding, easing proteolysis by proteinase K.
- Proprietary processes result in DNA-free proteinase K, well-suited in isolating DNA and RNA templates.
- Lot-to-lot consistency, superior purity and cost-efficiency in larger scales upon bulk request.
Applications of Recombinant Proteinase K
Proteinase K is commonly used in molecular biology to remove protein contamination from preparations of highly native, undamaged nucleic acid because it rapidly and effectively inactivates nuclease to prevent degradation of DNA or RNA. Such degradation is usually difficult to stop even with the presence of denaturing reagents.
Product Information
| Product Name | Proteinase K from Tritirachium album Limber, recombinant |
| Cat No. | NATE-1240 |
| CAS No. | 39450-01-6 |
| E.C. | 3.4.21.64 |
| Synonyms | Peptidase K, endoproteinase K, endopeptidase K |
| Source | From yeast cells with cloned gene encoding genetically engineered Engyodontium album (Tritirachium album) endolytic protease |
| Physical Appearance | Lyophilized powder |
| Molecular Mass | 29.3 kD |
| pI | 8.9 |
| pH Range | 4.5-12.0 (optimum pH range 7.5-11.5) |
| Purity | ≥95% (Native-PAGE) |
| Specific Activity | ≥34 U/mg protein |
| Unit Definition | One unit is defined as the enzyme activity that produces 1 μmol of tyrosine per minute from casein at 37°C, pH 7.5. |
| Storage Temperature | Recommended at -20 °C. |
| Temperature Profile | Maximum activity at 70°C, recommended at 37-70 °C. |
| DNA & RNA Contamination Assay | None detected. |
| DNase Contamination Assay | None detected. |
| RNase Contamination Assay | None detected. |
| Activators | 1-5 mM Ca2+ |
| Inhibitors | DIFP or PMSF |
| Shelf Life | Three years after delivery when stored sealed and dry below 4 °C. |
| Dilution Buffer Recommended |
20 mM Tris-HCl (pH 7.4), 1 mM CaCl2 or 20 mM Tris-HCl (pH 7.4), 1 mM CaCl2 and 2% glycerol |
| Storage Buffer | 20 mM Tris-HCl (pH 7.4), 1 mM CaCl2, 50% glycerol |
| Caution | The molecular biology grade lyophilized powder is not sterile. |
| Lot Size | Largest lot size available is 4 kg. Long-term and bulk supplies are available. |
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Creative Enzymes provides recombinant proteinase K from Tritirachium album Limber (Cat No. NATE-1240). The product has passed a series of quality control (QC) assays to ensure its high quality. Please do not hesitate to contact us if you have any further questions or specific needs.