The Tte UvrD Helicase, derived from the thermophilic bacterium Thermoanaerobacter tengcongensis, possesses the ability to unwind double-stranded DNA under high-temperature conditions. This enzyme is stable at 65°C and can be applied in isothermal amplification techniques without relying on single-strand binding proteins. In thermophilic Helicase-Dependent Amplification (tHDA), it assists polymerase in DNA strand separation, enabling isothermal amplification. Product Features: - Protein purity ≥95%;- Free of exonuclease, endonuclease, and RNase contamination;- Effectively eliminates non-specific amplification in LAMP systems. Figure: In the LAMP system, it effectively eliminates non-specific amplification. Two sets of LAMP primers were used to prepare LAMP reaction systems, with each set including an experimental group supplemented with 10 ng Tte UvrD Helicase and a control group without it. Figure1. Results showed that the addition of Tte UvrD Helicase effectively eliminated non-specific amplification in the LAMP system without affecting the detection of positive samples. Figure 2. Free of exonuclease, endonuclease, and RNase contamination. 20 ng of Tte UvrD Helicase was incubated with nucleic acid substrates, and band changes were analyzed via agarose gel electrophoresis. Experimental results showed that no exonuclease, endonuclease, or RNase contamination was detected in three batches of Tte UvrD Helicase.
