|Figure 1. Comparison of the SuperNuclease and other nucleases in different amount of nuclease by plasmid DNA cleavage assay. *The DNase I's activity unit is decided by the DNase I's definition.||Figure 2. Result shows the purity of SuperNuclease was approximately 98 %( SSNP01). The purity of each lot were determined by SDS-PAGE (12%) under reducing condition.|
|Figure 3. Benzonase Nuclease maintains high bio-activity at multiple temperatures, such as -20℃, 4℃and 37℃.||Figure 4. Compared with Trypsin-T4799, Benzonase Nuclease (SuperNuclease) has no typical protease activity.|
|SSNP01||SuperNuclease||> 98 % as determined by SDS-PAGE||< 0.22 EU/μg protein|
The SuperNuclease is a nonspecific nuclease with high activity, capable of completely digesting RNA and DNA (single stranded, double stranded, linear, circular and super coiled forms, that no fewer than five phosphate residues) into 5'-monophosphate-terminated oligonucleotides of 3-5 bases in length. SuperNuclease requires divalent cation, preferably Mg2+ for activity, displays a broad pH tolerance (range from 6 to 10, optimal at 8-8.5) and has a wide temperature optimum between 35℃ and 44℃. The nuclease is a homodimer (the dimer form is physiologic and functions more progressively than the monomer). Two disulfide bonds in the nuclease are crucial to its activity and stability. It does not have typical protease activity detected by azocasein assay. Its high intrinsic activity and broad substrate tolerance make the endonuclease an ideal tool in a variety of biotechnological and pharmaceutical applications. SuperNuclease can be removed by various purification methods.