A systematic exploration of citrullination at the proteome-wide level advances the understanding of its role in health and disease. Although mass spectrometry (MS) is a reliable and sensitive approach to pinpoint the citrullination sites, the abundance of citrullination is low, requiring enrichment to identify these sites comprehensively. Enrichment probes utilizing the reaction of glyoxal and citrulline provide specific enrichment of citrullinated proteins and peptides. However, this often results in lower fragmentation efficiency or missing site-specific information in MS. Here, we present an MS-compatible and cleavable chemical probe for the enrichment of citrullinated peptides, based on two commercially available compounds, making it readily accessible to the community to explore functional implications in diverse biological contexts. Citrullinated peptides were derivatized by 4-azidophenyl glyoxal, followed by a click reaction with dde-biotin alkyne that adds a biotin residue with a cleavable linker. After enrichment by streptavidin beads, the peptides are cleaved off, leaving a mass tag of 212 Da. The peptides were then measured in LC-MS/MS and analyzed by MSFragger using a custom variable modification. First, synthetic citrullinated peptides were used to optimize reaction conditions and spiked into a tryptic Hela digest to assess platform sensitivity in a complex background. The detection limit of a single peptide is ~780 fmol. Next, using an in vitro citrullinated Hela sample, the number of identified citrullinated peptides more than doubled after enrichment, with intensity-based enrichment of up to 90% for high citrullination content. Finally, extending its high-throughput capabilities in a 96-well format demonstrated reproducible quantitation in technical replicates. In conclusion, our method enhances the depth of the citrullination proteome and enables high-throughput application of citrullination analysis in clinical samples.