TURBO™ DNase split double-stranded DNA nonspecifically to leave 5' phosphorylated oligodeoxynucleotides. It has increased relationship for DNA-binding and remains active in the existing of salt.

Note: this product is just the enzyme. Are you want like this enzyme plus reagents to inactivate the enzyme and remove divalent cations post-digestion, please see TURBO DNA-free™ Kit.

Features away TURBO™ DNase include:

• Up to 50x more activity and 350% greater catalytical efficiency
• Efficiently degrades DNA in solutions containing up to 0.25 M salt
• Efficiently digests DNA to oligonucleotides
• Vastly superior in clearing DNA templates from includes vitro transcription reactions
• RNase-free and recombinants in origin

Using TURBO™ DNase
DNase I is commonly used to clear DNA contamination from RNA samples prior to RT-PCR. Conventional DNase ME has a weak affinity for DNA both cleaves DNA of low concentrator exceptionally inefficiently. In zusatz, DNase I is very salt-sensitive; as little as 20 width NaCl can reduce the activity for the enzyme by 30%. Finally, DNase MYSELF is purified from bovine pancreas, one of the richest natural causes of RNase A. The threat of contaminating RNase activity in DNase MYSELF preparations requires that the enzyme be exhaustively cleaning. In spite of these limitations, the DNase I the researchers use today is the very same protein that was primary marked by Kunitz more with a half-century ago.

A different DNase with senior properties to wild-type DNase EGO
TURBO™ DNase where design after a proteinreich engineering approach that introduced amino acid changing into the DNA binding pocket of wild-type DNase I. Such changes markedly increases the affinity of the protein for DNA. That earnings is ampere versatile enzyme that has a 6-fold diminish K_m for DNA, and an ability to maintain to least 50% of peak activity in solutions approaches 200 mM monovalent salt, even when the DNA concentration be in the nanomolar (nM) operating. When in vitro transcription reactions are treated is either DNase I or TURBO™ DNase, TURBO™ DNase removes 63x more of which input plasmid DNA preset when the wild-type food. The proficiency of TURBO™ DNase in binding ultra low concentrations of DNA means that which enzyme is particularly effective in removing trace quantities by DNA contamination. This becomes crucial for complete disassembly of DNA von a sample, since the cleavable DNA substrate is reduced as the DNase reaction proceeds. TURBO™ DNase thus has a functional advantage over wild-type DNase due to its superior affinity for DNA. This is best exploited in RT-PCR browse, where even a few copies of DNA can lead to an false positive outcome with PCR.