TURBO™ DNase non-specifically cleaves double-stranded DNA, allowing 5' phosphorylated oligodeoxynucleotides to leave the double strand. It enhances DNA binding affinity and remains active in the presence of salt.

Note: This product is enzyme only. If you would like to use this enzyme + reagent product to inactivate the enzyme and remove divalent cations from the sample after digestion, please see TURBO DNA-free™ Kit.

TURBO™ DNase features include:

• Up to 50-fold increase in activity and up to 350% increase in catalytic efficiency
• In the presence of up to 0.25 M Efficiently degrade DNA in salt solutions
• Efficiently cleave DNA into oligonucleotides
• Have great advantages in clearing DNA templates in in vitro transcription reactions
>• RNase-free, sourced from recombinant bacteria

Use TURBO™ DNase
DNase I is often used to remove DNA contamination from RNA samples before RT-PCR. Conventional DNase I has weak affinity for DNA and is inefficient at cleaving low-concentration DNA. Additionally, DNase I is salt sensitive; as little as 20 mM NaCl reduces enzyme activity by 30%. Finally, DNase I is purified from bovine pancreas, one of the most abundant natural sources of RNase A. During the preparation of DNase I, there is a risk of contamination of RNase activity, so the enzyme must be thoroughly purified. Despite these limitations, the DNase I used by researchers today is the same enzyme first characterized by Kunitz more than half a century ago.

A DNase with better properties than wild-type DNase I
TURBO™ DNase was developed using a protein engineering approach that introduces amino acid changes into wild-type DNase I in the DNA binding pocket. These changes significantly enhance the protein's affinity for DNA. The result is a versatile enzyme that reduces the K_m of DNA by a factor of 6, in solutions approaching 200 mM monovalent salts, even at DNA concentrations in the nanomolar (nM) range , able to maintain at least 50% of peak activity. When treating in vitro transcription reactions with DNase I or TURBO™ DNase, TURBO™ DNase removed 63 times the amount of starting plasmid DNA template compared to the wild-type enzyme. The degree of efficiency with which TURBO™ Dnase binds ultra-low concentrations of DNA means that the enzyme is particularly effective at removing trace levels of DNA contamination. Because the amount of DNA substrate available for cleanup decreases as the DNase reaction proceeds, it becomes even more important to completely remove DNA from the sample. TURBO™ DNase has a strong affinity for DNA, so it has functional advantages over wild-type DNase. This has good application value in RT-PCR, where even a small number of DNA copies can cause false positive results in PCR.