Proteomic profiling of MSC-derived EVs was performed on donor-matched samples. EV proteins were extracted in RIPA buffer containing a complete protease inhibitor cocktail, and total protein concentrations were quantified by BCA assay. Equal protein inputs (20–30 µg) were reduced, alkylated, and subjected to overnight trypsin digestion to generate MS-compatible peptide mixtures following established EV-proteomics workflows. Peptides were resolved by nano-LC and analyzed on a high-resolution Orbitrap mass spectrometer operated in data-dependent acquisition mode. Raw spectra were processed using standard pipelines, with peptide–spectrum matching against the human UniProt reference proteome using a target–decoy strategy. Protein identifications were restricted to a 1% false discovery rate at the peptide and protein levels and required ≥1 unique peptide, consistent with current mass-spectrometry reporting standards.