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

Item Type:	Article
Title:	Anti-c-myc antibody 9E10: epitope key positions and variability characterized using peptide spot synthesis on cellulose
Creators Name:	Hilpert, K. and Hansen, G. and Wessner, H. and Kuettner, G. and Welfle, K. and Seifert, M. and Hoehne, W.
Abstract:	The 9E10 antibody epitope (EQKLISEEDL) derives from a protein sequence in the human proto-oncogen p62 c-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.
Keywords:	Epitope Characterization, MAB 9E10, Myc-Tag, Peptide Spot Synthesis, Substitutional Analysis
Source:	Protein Engineering
ISSN:	0269-2139
Publisher:	Oxford University Press
Volume:	14
Number:	10
Page Range:	803-806
Date:	1 January 2001
Official Publication:	http://peds.oxfordjournals.org/cgi/content/abstract/14/10/803
PubMed:	View item in PubMed

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