| UNSPSC Code | 12352204 |
|---|---|
| eCl@ss | 32160410 |
| NACRES | NA.54 |
| Enzyme Commission (EC) Number | 3.4.21.62 ( BRENDA | IUBMB ) |
| MDL number | MFCD00132092 |
| biological source | Bacillus licheniformis |
| form | glycerol solution (50%) |
| specific activity | ≥7 units/mg protein (biuret) |
| concentration | ≥50 mg/mL |
| solubility | 0.85% sodium chloride: soluble, clear (Diluted) |
| storage temp. | 2-8°C |
| Quality Level | 200 |
Answer:It is a Bacillus licheniformis protease in a 50% glycerol solution, supplied as a 10 g package.
Answer:The specified minimum activity is 7 units per mg of protein under the defined assay conditions.
Answer:No. It catalyzes cleavage of peptide bonds; inhibitor reagents are used to reduce proteolysis rather than cause it.
Sigma-Aldrich protease from Bacillus licheniformis is a subtilisin-type protein-cleaving enzyme supplied as a 50% glycerol solution in a 10 g package. Proteases hydrolyze peptide bonds and are useful in controlled protein digestion, enzyme process studies and investigations of protein stability or degradation. This enzyme is distinct from a broad-spectrum protease inhibitor or a purified recombinant protein standard. The product has a stated specific activity of at least 7 units per milligram of protein under the defined activity assay conditions; that activity value is not equivalent to a universal working concentration. Glycerol contributes to the formulation and must be considered when preparing reaction dilutions or comparing with dry enzyme preparations. Choose substrate, buffer, temperature, incubation time and enzyme dose in relation to the experimental endpoint, then terminate the reaction using a validated method. Include substrate blanks and enzyme-free controls, and handle protease solutions carefully to prevent unintended digestion of laboratory proteins and biological samples. Consult lot documentation for quantitative assay requirements.
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