The 4G10, pY20 and p-TYR-100 antibody specificity: profiling by peptide microarrays.

Michele Tinti, Aurelio Pio Nardozza, Emanuela Ferrari, Francesca Sacco, Salvatore Corallino, Luisa Castagnoli, Gianni Cesareni

Department of Biology, University of Rome Tor Vergata, Via della ricerca scientifica, 00133 Rome, Italy.

New biotechnology 2012 Jun 15

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The reversible phosphorylation of tyrosine residues is one of the most frequent post-translational modifications regulating enzymatic activities and protein-protein interactions in eukaryotic cells. Cells responding to internal or external regulatory inputs modify their phosphorylation status and diseased cells can often be diagnosed by observing alterations in their qualitative or quantitative phosphorylation profile. As a consequence the ability to describe the phosphorylation profile of a cell is central to many approaches aiming at the characterisation of signalling pathways. Anti-phosphotyrosine (pY) antibodies are widely used as experimental tools to monitor the phosphorylation status of a cell. By using peptide microarray technology we have characterised the substrate specificity of three widely used pY antibodies. We report that they are more sensitive to sequence context than is generally assumed and that their sequence preferences differ. Copyright © 2012 Elsevier B.V. All rights reserved.

Citation

Michele Tinti, Aurelio Pio Nardozza, Emanuela Ferrari, Francesca Sacco, Salvatore Corallino, Luisa Castagnoli, Gianni Cesareni. The 4G10, pY20 and p-TYR-100 antibody specificity: profiling by peptide microarrays. New biotechnology. 2012 Jun 15;29(5):571-7