Power Taq DNA Polymeraseis a derivative of Taq DNA-Polymerase. It is a 5`-exo-minus Nterminally truncated Thermus aquaticus DNA polymerase. As expressed from a gene contruct in E. coli, translation initiates a Met236, bypassing the 5`-3`exonuclease domain of the DNA polymerase-encoding gene. The enzyme reveals a highly active and even more heat-stable DNA polymerase activity of to compare with Taq DNA polymerase. The optimal range of Mg²+ concentration for Power Taq DNA Polymerase is broader than for the majority fo thermostable polymerases. This feature allows to optimize reaction conditions easier then for other polymerases. Repeated exposure to 98 °C does not diminish the enzyme activity. Significant activity remains even after exposure to 99°C.
