| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Biological Activity | |
| Enzyme Type | |
| Expression System | |
| Form | Lyophilized |
| Formulation | |
| Product Type | |
| Purity | |
| Source | Yeast |
| Species | |
| Storage | |
| Target |
Product Description
Tritirachium album Proteinase-K Recombinant
Overview
The Proteinase K enzyme is a member of the Peptidase family S8. Proteinase K is a broad-spectrum serine protease. Proteinase K is capable of digesting hair (keratin), henceforth, the name "Proteinase K". Proteinase K is activated by calcium, the enzyme digests proteins especially after hydrophobic amino acids (aliphatic, aromatic and other hydrophobic amino acids). Proteinase K is frequently utilized in molecular biology to digest protein and remove contamination from preparations of nucleic acid. Addition of Proteinase K to nucleic acid preparations rapidly inactivates nucleases which may otherwise degrade the DNA or RNA during purification. Proteinase K is greatly fitting to this application as the enzyme is active in the presence of chemicals which denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is utilized for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, given that it quite effectively inactivates DNases and RNases.
Biological Activity
36 Units/mg.One unit is defined as the amount of enzyme that will hydrolyze urea-denatured hemoglobin to produce color equivalent to 1.0 mol tyrosine per min at 37°C, pH 7.5 (color by Folin-Ciocalteu reagent).
Specifications
| Purity | Greater than 95% as determined by SDS-PAGE. |
|---|---|
| Formulation | The Proteinase-K was lyophilized without any additives. |
| Storage | Recombinant Proteinase-K although stable at room temperature, should be stored between 2-8°C. Do not freeze! |
| Expression System | Yeast |
