The presentation will follow a logical sequence of how anti-EGFR antibodies are generated and modified to make them cytotoxic for tumor cells with high levels of EGFR or the variant EGFRvIII. It will specifically focus on beginning with a key mouse monoclonal antibody termed ‘40H3’ and then the transition to the humanization of this antibody to produce the antibody termed ‘A10.’ These anti-EGFR antibodies can be used as either independent agents or targeting domains in recombinant immunotoxins (RITs), antibody-drug conjugates (ADCs), bispecific antibodies, and chimeric antigen receptors (CARs). Attendees will have an opportunity to ask questions.
About the Featured Technology
Dr. Fitzgerald and his team established that using one of the antibodies (40H3) as an antibody-drug conjugate has potential use as a potent therapeutic because of its ability to kill both breast cancer cells and epidermoid cancer cells and reduce tumor growth in mice. The 40H3 antibody is also able to bind to EGFR when overexpressed in cancers of various tissue origins and thus has broad therapeutic potential for a wide cancer patient population. Further, the 40H3 antibody has been humanized producing an antibody termed ‘A10’ which retains the full binding activity of 40H3.
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Who Should Attend?
Business development professionals
Drug development professionals
Investors and entrepreneurs
Foundations, philanthropies and patient advocacy groups
David Fitzgerald, Ph.D.
Laboratory of Molecular Biology
Center for Cancer Research (CCR)
National Cancer Institute