Protein carbonylation, known as one of the most harmful oxidative post-translational modifications (PTMs), plays a significant role in aetiology and/or progression of several pathological conditions.1-2 Basically, the high level of reactive oxygen species (ROS) induced by redox imbalance in pathological states are deemed to be the main cause of protein carbonylation. The oxidative PTMs initiated by ROS is an irreversible modification, resulting in protein degradation, and involves the formation of aldehyde-, ketone-, or lactam-groups at the side chains of amino acid residues. Hence, the development of effective probes to detect the protein carbonylation in situ has become a research focus in recent years. Hydrazine derivates are most widely used to identify the specific proteins that are carbonylated since 2,4-dinitrophenyl hydrazine (DNPH) was firstly introduced by Levine et al.3 However, most of the current tools are only suitable for fixed cells or tissues. Herein, we design two AIE-active compounds aided by hydrazine group, which have opened up new possibilities for imaging the carbonylated protein in live cells as well as further analysis utilizing mass spectrometry (MS)-based proteomics. In this poster, we will present our recent progress in synthesis and application of tetraphenylethylene-cored carbonylated protein probes.