Identification of the epitope for the epidermal growth factor receptor-specific monoclonal antibody 806 reveals that it preferentially recognizes an untethered form of the receptor.

@article{Johns2004IdentificationOT,
  title={Identification of the epitope for the epidermal growth factor receptor-specific monoclonal antibody 806 reveals that it preferentially recognizes an untethered form of the receptor.},
  author={Terrance G Johns and Thomas P. J. Garrett and Jennifer R. Cochran and Nathan E. Hall and Peter A. Hoyne and Mark Jon Olsen and Yong-Sung Kim and Julie Rothacker and Edouard Collins Nice and Francesca Dominique Walker and Gerd Ritter and Achim A. Jungbluth and Lloyd J. Old and Colin W. Ward and Antony W. Burgess and K Dane Wittrup and Andrew Mark Scott},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 29},
  pages={
          30375-84
        }
}
The epidermal growth factor receptor (EGFR) is overexpressed in many epithelial cancers, an observation often correlated with poor clinical outcome. Overexpression of the EGFR is commonly caused by EGFR gene amplification and is sometimes associated with expression of a variant EGFR (de2-7 EGFR or EGFRvIII) bearing an internal deletion in its extracellular domain. Monoclonal antibody (mAb) 806 is a novel EGFR antibody with significant antitumor activity that recognizes both the de2-7 EGFR and a… CONTINUE READING
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