In vivo and in vitro activity of an immunoglobulin Fc fragment (Fcab) with engineered Her-2/neu binding sites.

@article{Woisetschlger2014InVA,
  title={In vivo and in vitro activity of an immunoglobulin Fc fragment (Fcab) with engineered Her-2/neu binding sites.},
  author={Max Woisetschl{\"a}ger and Bernhard Antes and Radha Borrowdale and Susanne Wiederkum and Manuela Kainer and Herta Steinkellner and Gordana Wozniak-Knopp and Kevin Moulder and Florian R{\"u}ker and Geert Cornelius Mudde},
  journal={Biotechnology journal},
  year={2014},
  volume={9 6},
  pages={844-51}
}
Antigen-binding Fc fragments (Fcabs) are a new unique class of immunotherapeutics. They are small (50 kD) fully functional antibody alternatives that bind antigen and elicit effector functions such as antibody-dependent cytotoxicity (ADCC) and complement-dependent cytotoxicity. Since Fcabs carry the natural FcRn binding site of antibodies, they have very favorable pharmacokinetics. We showed recently that Fcab H10-03-6 is a high-affinity binder of Her-2/neu (ErbB2/neu) mediating killing of Her… CONTINUE READING
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