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| Product Name | Thermolabile Proteinase K, Heat-Labile (120 U/mL) |
| Catalog No. | IVDRM-0590 |
| Description | A genetically engineered serine protease with broad cleavage activity, Thermolabile Proteinase K hydrolyses a wide range of peptide bonds and, unlike other proteinase K preparations that are only partly inactivated on heating, it is inactivated by 10 minutes at 55°C. That heat-labile character lets the enzyme be used in the same vessel as the following enzymatic step, avoiding any extra purification to remove it. It keeps the activity and specificity of the wild-type enzyme and cuts peptide bonds mostly on the carboxyl side of amino acid residues with a preference for aliphatic and aromatic residues. The usual working concentration is 2 to 4 U/mL, adjusted for buffer composition, SDS or urea content, pH and temperature. |
| Intended Use | Protein digestion and nucleic acid removal in nucleic acid extraction and purification workflows |
| Principle / Technology | Broad specificity serine protease digestion of peptide bonds with heat inactivation at 55°C |
| Sample Type | Protein contaminants in nucleic acid extraction and purification |
| Specificity | Heat labile and fully inactivated at 55°C in 10 minutes; broad peptide bond specificity |
| Reaction Conditions / Protocol | Use at a working concentration of 2 to 4 U/mL and inactivate by heating at 55°C for 10 minutes |
| Storage Conditions | -25 to -15°C |
| Shelf Life | 2 years |
| Package Specifications | 30 U; 120 U |
| Key Features | Heat-labile inactivation at 55°C allows one-tube workflows; wild-type-like activity and specificity |
| Concentration | 120 U/mL |
| Readouts / Downstream Assays | Protein removal and downstream nucleic acid yield or purity |
For in vitro diagnostic use.
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