Saltonase is a cold-active, heat-labile recombinant endonuclease produced in E.coli. Saltonase originates from psychrophilic bacteria and effectively digests all types of DNA and RNA substrates in different buffer conditions and a broad range of temperatures. It is very active in demanding conditions, including low temperatures and environment with high salt content. These features make Saltonase extremely useful for removing undesired nucleic acids contamination during purification of proteins in laboratory and manufacturing workflows.
Features and advantages
- Highly active in a broad range of temperatures (>20% at 8 – 45°C).
- Extreme nucleolytic activity at high salt concentrations (optimal concentration range for NaCl or KCl is 0 – 1.1 M), and other buffer additives, which can significantly improve efficiency and purification yield in various workflows.
- Highly active in the typical buffers and grow media.
- Requires ≥ 1 mM Mg2+ to activate and shows a broad spectrum of pH activity (optimum at pH 7.5 – 9.0).
- Irreversible thermal inactivation at low temperature (15 min at 52°C in the presence of 1 mM DTT).
- Purification of biologics from residual nucleic acids in biopharma manufacturing.
- Purification of recombinant proteins and enzymes for research and diagnostic use.
- Removal of undesired nucleic acids contamination in molecular biology reagents in demanding systems.
- Reduction of viscosity in biological samples (during production, automation).
One unit (U) is defined as the amount of enzyme that causes an increase in absorbance at 260 nm of 1.0 in 30 minutes at 37°C in 50 mM Tris-HCl buffer, pH 8.0 (25°C) supplemented with 5 mM MgCl2, 0.1 mg/ml BSA and 0.5 mg/ml herring sperm DNA as a substrate.