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Protein Engineering, Vol. 14, No. 10, 803-806, October 2001
© 2001 Oxford University Press

Anti-c-myc antibody 9E10: epitope key positions and variability characterized using peptide spot synthesis on cellulose

K. Hilpert1, G. Hansen1, H. Wessner1, G. Küttner1, K. Welfle2, M. Seifert3 and W. Höhne4

1 Institut für Biochemie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Monbijoustr. 2, 10117 Berlin, 2 Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Straße 10, 13122 Berlin, 3 Institut für Medizinische Immunologie, Universitätsklinikum Charité,Humboldt-Universität zu Berlin, Monbijoustr. 2, 10117 Berlin, Germany

The 9E10 antibody epitope (EQKLISEEDL) derives from a protein sequence in the human proto-oncogen p62c-myc and is widely used as a protein fusion tag. This myc-tag is a powerful tool in protein localization, immunochemistry, ELISA or protein purification. Here, we characterize the myc-tag epitope by substitutional analysis and length variation using peptide spot synthesis on cellulose. The key amino acids of this interaction are the core residues LISE. The shortest peptide with a strong binding signal is KLISEEDL. Dissociation constants of selected peptide variants to the antibody 9E10 were determined. scFv constructs with the shortest possible myc-tags were successfully detected by Western blot and ELISA, giving a signal comparable to that of the original myc-tag.


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