Glutathione Proteomics Service

Protein S-glutathionylation (SSG) is a crucial reversible post-translational modification reaction that plays a key role in cellular redox regulation. During this modification, the thiol group of glutathione (GSH) forms a disulfide bond with the thiol group of cysteine residues in proteins, thereby altering protein structure, activity, and functional state.
Biological Significance:
- Protein Protection: Under oxidative stress, S-glutathionylation can protect cysteine residues from irreversible over-oxidation
- Protein Function Regulation: Through dynamic changes in modification and demodification, it regulates protein enzymatic activity, structure folding, cellular localization, and protein-protein interactions
- Redox Homeostasis Maintenance: Participates in cellular redox balance maintenance, closely linked to signal transduction, metabolic regulation, transcription, translation, and other life activities
- Disease Relevance: Intimately associated with tumorigenesis, neurodegenerative diseases, cardiovascular diseases, metabolic disorders, and aging processes
To date, over 2,000 proteins have been identified to carry S-glutathionylation modifications, involving metabolism, transcription and translation, protein folding, free radical scavenging, cell cycle control, and other biological functions.
Service Offerings
| Service Name |
Primary Function |
Deliverables |
| Panoramic Glutathionylated Protein Identification |
Systematically identify all S-glutathionylated proteins and their modification sites at the proteome level |
- List of glutathionylated proteins and modification sites
- GO functional classification and KEGG pathway enrichment analysis
- Modification site sequence characteristics and conservation analysis
|
| Glutathionylation Modification Quantification |
Precisely measure relative/absolute changes in S-glutathionylation levels across different sample conditions |
- Relative quantification ratios of modified proteins between conditions
- Quantitative information and statistical analysis of modification sites
- Identification and functional annotation of differential modified proteins
|
| Target Protein Deep Targeted Analysis |
Conduct in-depth analysis on known or potential target proteins to comprehensively identify all glutathionylation modification sites |
- Complete modification site map of target protein
- 3D structure and functional domain localization information of modification sites
- Analysis of potential impacts on protein structure and function
|
| Multi-Type Redox Modification Combined Analysis |
Simultaneously detect multiple thiol-based redox modifications to reveal interactions and dynamic conversions between different modifications |
- Synchronized detection data of multiple redox modifications
- Analysis of cross-regulatory relationships between modifications
- Redox signal pathway network map
|
Service Advantages
- Precise and Efficient Modification Identification
Utilizing high-resolution liquid chromatography-mass spectrometry (LC-MS/MS) technology combined with multi-level enrichment strategies, we accurately identify specific glutathionylation sites on proteins. A single experiment can simultaneously identify hundreds to thousands of modification sites, providing comprehensive panoramic analysis.
- Reliable Quality Assurance
Rigorous sample quality assessment, standardized operational procedures, and comprehensive data quality verification mechanisms ensure the reliability and reproducibility of experimental results.
- Deep Biological Interpretation
Our comprehensive bioinformatics analysis transforms raw mass spectrometry data into meaningful biological discoveries, including functional annotation, pathway analysis, protein interaction networks, and data integration.
- Thoughtful Professional Service
We flexibly design personalized solutions based on your research needs, providing full-cycle professional consultation and technical support from sample preparation through experimental optimization to data interpretation.
Workflow
Receive and verify samples, perform protein extraction and concentration quantification
Chemically label samples, enrich glutathionylated proteins through affinity purification, and further digest proteins into peptides
Separate peptides using liquid chromatography, detect samples with LC-MS/MS, and collect data
Process raw mass spectrometry data, identify peptide information, determine protein identity and modification sites
Perform functional analysis and pathway annotation of modified proteins, conduct quality control and result verification
Compile all data and analysis results, generate comprehensive final report
Whether your research aims at exploring disease mechanisms, discovering drug targets, or investigating protein function regulation, we provide professional technical support and reliable data quality assurance. Choose our service and make your research more efficient, more precise, and more insightful.
The service is for research only, not for clinical use.