Proteinase K
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IVD Raw Materials
| Z02003 | |
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| Ask us a question | |
Protease K is a subtilian-type protease isolated from the saprophytic fugus Tritirachium album. It is particularly suitable for short digestions. It possesses a very broad peptide cleavage activity, which remains stable over a wide range of temperatures and pH values, although its activity increases at higher temperature. |
Proteinase K;
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| Source | Tritirachium album |
| Biological Activity |
>30 units/mg protein (hemoglobin, pH7.5, 37oC) Unit Definition: It is the amount of enzyme which releases at 37 oC in 1 min as many folin-positive amino acid and peptides from hemoglobin as 1umol of tyrosine. |
| Reconstitution | Reconstitute lyophilized Proteinase K in ddH2O at 1 mg/ml and yield a clear colorless solution. |
| QC |
Purified by chromatography RNases: Not detectable DNases: Not detectable Exonucleases: Not detectable |
| Usage | In presence of 0.5-1.0% SDS, Proteinase K inactivates DNases and RNases in eukaryotic and microbiological cell cultures. The use of Proteinase K during lysis of the cells allows the isolation of intact highly-molecular nucleic acids. |
| Storage & Stability | Lyophilized recombinant Proteinase K remains stable up to 3 years at -20°C. Upon reconstitution, Proteinase K should be stable up to 1 year at -20°C. |
| Key Features | Proteinase K is a highly active and stable protease with low cutting specificity. The enzyme belongs to the group of subtilisine-related serine proteases and is strongly inhibited by PMSF. |
| See datasheet for details. |