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High-resolution MS capability : Sub-ppm mass accuracy and deep proteome coverage enabled by Orbitrap Fusion Lumos and Q Exactive HF platforms Optimized enrichment workflow : GSH-targeted capture strategy enhances signal-to-noise ratio and recovers low-abundance S-glutathionylation sites Multi-PTM analysis compatibility : Supports co-enrichment and analysis with phosphorylation, ubiquitination, and nitrosylation for PTM crosstalk mapping End-to-end project adaptability : Flexible options for sample preparation, experimental design, and data reporting tailored to research needs Broad sample compatibility : Applicable to cell lysates, tissues, plasma/serum, and purified proteins across various biological systems Applications Our S-Glutathionylation Proteomics Service supports multiple research and preclinical use cases: Redox and stress signaling: Characterize dynamic redox-sensitive cysteine modifications under oxidative challenge Disease mechanism exploration: Construct SSG modification maps in models of cardiovascular, oncological, or neurodegenerative diseases Drug response and antioxidant evaluation: Track SSG shifts in response to GSH modulators, redox-targeted therapies, or dietary interventions Environmental toxicology: Study S-glutathionylation changes in response to pollutants, radiation, or chemical exposures Biomarker discovery: Identify site-specific SSG events with diagnostic or therapeutic potential Case Study Case 1: Mapping S-glutathionylation on Cardiac Myosin via Top-Down Proteomics In a study, researchers applied top-down mass spectrometry to map endogenous S-glutathionylation (SSG) on ventricular myosin light chain-1 (MLC-1v)

It is interdisciplinary in nature, drawing from disciplines including psychology, ethology, anthropology, evolution, zoology, archaeology, and population genetics (Wilson 2000)

Preler H, Machule ML, Ufer F, Bnger I, Li LY, Buchholz E, et al

[DOI] [PMC free article] [PubMed] 129.Prince PSM
