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

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)571-577
Number of pages7
JournalNew Biotechnology
Issue number5
Publication statusPublished - Jun 15 2012

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology
  • Bioengineering


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