Expression and detection strategies for an scFv fragment retaining the same high affinity than Fab and whole antibody: Implications for therapeutic use in prion diseases.

@article{PadiolleauLefevre2007ExpressionAD,
  title={Expression and detection strategies for an scFv fragment retaining the same high affinity than Fab and whole antibody: Implications for therapeutic use in prion diseases.},
  author={S{\'e}verine Padiolleau-Lefevre and Coralie Alexandrenne and Fatima Dkhissi and Gilles Clement and Sosth{\`e}ne S. Essono and C{\'e}line Blache and Jean-Yves Couraud and Anne Wijkhuisen and Didier Boquet},
  journal={Molecular immunology},
  year={2007},
  volume={44 8},
  pages={1888-96}
}
Since antibodies currently constitute the most rapidly growing class of human therapeutics, the high-yield production of recombinant antibodies and antibody fragments is a real challenge. Using as model a monoclonal antibody directed against the human prion protein that we prepared previously and tested for its therapeutic value, we describe here experimental conditions allowing the production of large quantities (up to 35 mg/l of bacterial culture) of correctly refolded and totally functional… CONTINUE READING

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