Cycling probe technology with RNase H attached to an oligonucleotide.

@article{Bekkaoui1996CyclingPT,
  title={Cycling probe technology with RNase H attached to an oligonucleotide.},
  author={Faouzi Bekkaoui and I Poisson and Warren Crosby and Lynn Pomeroy - Cloney and Paul J. Van Duck},
  journal={BioTechniques},
  year={1996},
  volume={20 2},
  pages={240-8}
}
A streptavidin-RNase H gene fusion was constructed by cloning the Thermus thermophilus RNase H coding sequence in the streptavidin expression vector pTSA18F. The gene was expressed in Escherichia coli, and the resulting fusion protein was purified to apparent homogeneity. The fusion protein was shown to have a molecular weight of 128 kDa and to consist of four subunits. Furthermore, heat treatment of the fusion enzyme showed that it was stable as a tetramer at 65 degrees C. The fusion enzyme… CONTINUE READING