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TURBO DNase: Hyperactive, Salt Tolerant DNase


Up to 50X more activity and 350% greater catalytic efficiency than conventional DNase I

Removes trace quantities of DNA that can plague RT-PCR

RNase-free and recombinant in origin: Purified from a source that is 107-fold lower in RNase activity than bovine pancreas


A New Hyperactive DNase with Superior Properties to Wild-type DNase I
TURBO DNase (patent pending) was developed using a protein engineering approach that introduced amino acid changes into the DNA binding pocket of wild-type DNase I. These changes lower the Km for DNA by 6-fold, compared to wild type (wt) DNase I. In addition, TURBO DNase retains at least 50% of peak activity in solutions approaching 200 mM monovalent salt, even when the DNA concentration is in the nanomolar (nM) range. Wild type DNase I in comparison, loses significant activity when the salt level reaches 20 mM NaCl. Thus, TURBO DNase is extremely efficient at removing DNA from many common molecular biology buffers, such as in vitro transcription buffer (Figure 1). In this case, TURBO DNase reduces the input 50 kb lambda DNA to digested fragments that are roughly 100 times smaller than those treated with conventional DNase I. As a result, TURBO DNase is the enzyme of choice for eliminating plasmid DNA templates from transcription reactions, particularly for the synthesis of RNA standards used in RT-PCR and generating RNA for microinjection and transfection experiments.

Figure 1. TURBO DNase Provides Superior Elimination of DNA from in vitro Transcription Reacti
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