Setting up of an innovative procedure for redox proteomics and its application for definition of the redox status of a cellular model.

Human proteome contains 214.000 cysteine residues. In the subset of protein not-free thiols, these are alkylated or, most frequently, oxidized. While disulfides, the largely most abundant oxidized form, have a pivotal role in driving protein folding, recently, their reversible formation also came to the stage as the final outcome of cell signaling pathways under the control of the nucleophilic/electrophilic tone. Specific high throughput procedures, collectively known as redox proteomics, have been developed to pinpoint these functional redox transition. Here we present an approach for pairwise comparison, integrating differential labeling with cys reactive probes and chromatographic isolation of redox sensitive proteins.