Binding kinetics of antiricin single domain antibodies and improved detection using a B chain specific binder.

@article{Anderson2010BindingKO,
  title={Binding kinetics of antiricin single domain antibodies and improved detection using a B chain specific binder.},
  author={George P. Anderson and Rachael D. Bernstein and Marla D. Swain and Dan Zabetakis and Ellen R. Goldman},
  journal={Analytical chemistry},
  year={2010},
  volume={82 17},
  pages={7202-7}
}
Single domain antibodies are the recombinantly expressed binding fragments derived from heavy chain antibodies found in camels and llamas. These unique binding elements offer many desirable properties such as their small size ( approximately 15 kDa) and thermal stability, which makes them attractive alternatives to conventional monoclonal antibodies. We created a phage display library from llamas immunized with ricin toxoid and selected a number of single domain antibodies. Phage selected on… CONTINUE READING
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