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DNase I (RNase Free)

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DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides. It acts on single-stranded DNA, double-stranded DNA, and even chromatin. The optimal working range is pH 7-8, and the activity of DNase depends on Ca2+, and can be activated by divalent metal ions such as Co2+, Mn2+, Zn2+. 5 mM Ca2+ protects the enzyme from hydrolysis. In the presence of Mg2+, the enzyme can randomly recognize and cut off any site on any strand of DNA. While in the presence of Mn2+, two strands of DNA can be recognized simultaneously and cut at almost the same site. DNase I was first isolated from the pancreas, and to date the mammalian pancreas is still one of the main sources of this enzyme.


Ice bag transportation. The freeze-dried powder can be stored at -20℃ for 2 years.


After adding EDTA to the final concentration of 2.5 mM, heating at 65℃ for 10 min can inactivate DNase I. Phenol-chloroform extraction can also inactivate DNase I. Metal ion chelators, zinc ions up to mM/L concentration, reductants such as 0.1% SDS, DTT, mercaptoethanol, and salt concentrations above 50-100 mM all have significant inhibitory effects on DNase I.

Only for research and not intended for treatment of humans or animals

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