Cat. No. / ID: Not Applicable
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 an environment with high salt content. These features make Saltonase extremely useful for removing undesired nucleic acid contamination during the purification of proteins in laboratory and manufacturing workflows.
It is supplied with 20 mM Tris-HCl pH 7.5; 500 mM NaCl; 5 mM MgCl2; 50% (v/v) glycerol.
One unit 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.
|Protease activity||None detected|
Saltonase cleaves nucleic acids (NA) into fragments below 10 nucleotides (nt). It remains active even at 0°C and in a high salt-content environment. It is particularly applicable for removing contaminating nucleic acids during the purification of different proteins in laboratory and manufacturing workflows. Saltonase is produced with the use of animal origin-free materials.
Protein purity is determined using assay by SDS-PAGE electrophoresis resulting in >90% purity.
This is used for applications such as: