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| Product Name | Thermolabile Proteinase K (Recombinant, 120 U/mL) |
| Catalog No. | IVDRM-0224 |
| Description | This product is a genetically engineered, recombinant serine protease with broad cleavage activity that hydrolyzes a variety of peptide bonds. Unlike other proteinase K enzymes that can only be partially inactivated by heating, this thermolabile proteinase K can be completely heat-inactivated by incubation at 55 °C for 10 minutes. This allows subsequent enzymatic steps to be performed in the same reaction vessel, enabling a simpler, more efficient workflow without additional purification steps to remove the enzyme. The enzyme retains activity and specificity similar to the wild-type version, cleaving peptide bonds primarily on the carboxyl side of most amino acid residues, with some preference for aliphatic and aromatic amino acids. The commonly used working concentration is 2-4 U/mL; the exact working concentration should be determined according to buffer composition (SDS, urea), pH, temperature, and other factors. |
| Intended Use | Protein digestion in molecular biology and diagnostic workflows, e.g., proteolytic inactivation of enzymes such as restriction endonucleases and sample digestion during nucleic acid extraction, where subsequent complete heat inactivation of the protease is desired. Enables downstream enzymatic steps in the same reaction vessel without enzyme removal. |
| Principle / Technology | Broad-specificity recombinant serine protease that hydrolyzes peptide bonds, mainly on the carboxyl side of most amino acid residues, with preference for aliphatic and aromatic amino acids. Engineered for heat lability so it can be fully inactivated at 55 °C for 10 min. |
| Performance Range / Specifications | Strong digestion capacity; completely heat-inactivated by incubation at 55 °C for 10 min. Effectively inactivates restriction endonucleases (e.g., PvuII) without affecting proteins added to the subsequent reaction system after heat inactivation. No detectable exonuclease, nickase, or RNase residues (verified across three batches by agarose gel electrophoresis of nucleic acid substrates incubated with 0.12 U of enzyme). |
| Specificity | Cleaves peptide bonds primarily on the carboxyl side of most amino acid residues, with some preference for aliphatic and aromatic amino acids; activity and specificity similar to the wild-type enzyme. |
| Reaction Conditions / Protocol | Common working concentration: 2-4 U/mL; the exact working concentration depends on buffer composition (presence of SDS, urea), pH, temperature, and other factors. Heat inactivation: incubate at 55 °C for 10 min. |
| Storage Conditions | Store at -25 to -15 °C. |
| Shelf Life | 2 years |
| Package Specifications | 30 U 120 U |
| Product Form | Liquid |
| Quality Control | No detectable exonuclease, nickase, or RNase residues; consistent quality verified across three batches by agarose gel electrophoresis with nucleic acid substrates. |
| Concentration | 120 U/mL |
| Source / Origin | Recombinant; genetically engineered serine protease. |
| Compatibility | Subsequent enzymatic steps can be carried out in the same reaction vessel after heat inactivation, without additional purification steps to remove the enzyme; heat inactivation has no impact on proteins subsequently added to the reaction system. |
| Batch-to-Batch Consistency | Three independent batches showed no detectable exonuclease, nickase, or RNase residues, ensuring accuracy and reliability of experimental results. |
| Heat Inactivation | 55 °C for 10 min (complete inactivation) |
For research use only, not for clinical use.
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