Protein Sulfenylation Detection Service
Protein sulfenylation is an important post-translational modification that occurs on cysteine residues within protein molecules. When cells experience mild oxidative stress, the cysteine thiol groups (-SH) in proteins are oxidized to sulfenic acid groups (-SOH), creating reversible, dynamically regulated protein functional modifications. This process has unique biological significance: sulfenic acids can serve as transient intermediates, further transforming into other oxidative modification forms such as disulfide bonds and sulfinic acids. They can also function directly as protein switches, reversibly regulating protein structure and biological activity. Under strong oxidative stress conditions, sulfenic acids can be further oxidized into relatively irreversible sulfinic acids (-SO2H) or sulfonic acids (-SO3H), which persist in proteins as lasting damage markers.
Figure 1. The formation of protein cysteine sulfenic acid. (Source: Mu B, et al. 2024)
Protein sulfenylation levels not only accurately reflect the intensity of redox signals in biological systems but also hold significant value in exploring pathological mechanisms associated with oxidative stress. As a sensitive biomarker of cellular redox homeostasis, this modification is crucial for revealing the molecular mechanisms underlying tumor development and progression, cardiovascular disease, aging-related diseases, and neurodegenerative disorders. By deeply analyzing the dynamic changes in sulfenylation patterns, researchers can gain a better understanding of disease pathology, thereby opening new avenues for drug development and clinical diagnostics.
Our Services
| Service Category | Service Description |
| Comprehensive Protein Sulfenylation Detection | We employ high-resolution mass spectrometers combined with chemical labeling strategies for multifaceted identification and quantitative analysis at both protein and peptide levels. Through sulfenic acid-specific probe labeling followed by high-resolution LC-MS/MS, we accurately identify modification sites and quantify modification levels. |
| Personalized Sample Processing | We handle different sample types—tissues, serum, cells, and more—with tailored preparation protocols including sample stabilization, lysis, protein extraction, and enzymatic digestion. Our approach maximizes the preservation of authentic protein modification states while minimizing artificial oxidation artifacts during sample preparation. |
| Multi-level Quantitative Analysis | We provide absolute quantification using isotope-labeled internal standards, relative quantification through multi-sample comparisons, and site-specific analysis to pinpoint the exact cysteine residues where modifications occur. |
| In-depth Data Mining and Interpretation | We conduct functional annotation of modified proteins, signal pathway enrichment analysis, and correlate oxidative stress biomarkers with sample clinical features and phenotypic data, generating visualized modification profiles and heatmaps. |
| Extended Application Services | We support multi-omics integrated analysis combining sulfenylation data with transcriptomics and metabolomics, biomarker validation in disease cohorts, and drug target identification with efficacy assessment. |
Why Choose Us
- Advanced Technical Platform
Our facility is equipped with cutting-edge high-resolution mass spectrometry instruments featuring exceptional analytical precision. We have established a comprehensive library of chemical labeling reagents and robust bioinformatics analysis pipelines, with detection selectivity and specificity thoroughly optimized for sulfenylation modifications. - High-Fidelity Sample Processing
We maintain rigorous low-temperature handling, rapid sample processing, and multiple quality checkpoints throughout to prevent artificial modifications during preparation. Using techniques such as rapid cell freezing with liquid nitrogen and vacuum freeze-drying, we preserve the authentic modification state of proteins while ensuring excellent data reproducibility. - Streamlined Workflow
Our automated sample preparation combined with online liquid chromatography separation and mass analysis increases detection throughput and sensitivity. We have established quality control measures at both protein and peptide levels, significantly reducing turnaround time from sample receipt to final report. - Diverse Sample Compatibility
We can handle a wide range of biological sample types, including animal tissues, plant materials, microbial cells, and cell pellets as solid samples, as well as serum, plasma, urine, cerebrospinal fluid, and secreted proteins as liquid samples.
Workflow
We communicate with you about sample characteristics and research objectives, then design optimal protocols for sample preparation, labeling, and detection based on your specific needs, providing detailed cost estimates and timelines.
We receive and verify samples for completeness and proper storage conditions, measure protein concentration and assess quality, and perform any necessary pre-processing steps.
We apply optimized protein extraction protocols, use highly specific probes to form covalent adducts with sulfenic acid groups, and perform precise protein digestion.
We conduct online liquid chromatography separation and high-resolution mass spectrometry analysis, monitor system performance in real-time, and perform multiple replicate measurements for each sample to ensure reliable results.
We use professional databases and software for peptide identification, modification site mapping, and quantitative calculations, followed by statistical analysis and biological interpretation.
We prepare comprehensive reports including sample information, technical methods, key parameters, and data visualizations, providing raw data files and detailed figures along with follow-up consultation.
Sample Submission Guidelines
Sample Collection and Storage Requirements
- Avoid freeze-thaw cycles: Freeze samples once only—repeated thawing compromises data quality
- Sterile collection: Use sterile tools to collect samples and prevent microbial contamination
- Short-term storage (< 1 week): -20°C freezer or 4°C cold storage
- Long-term storage (> 1 week): -80°C freezer
- Special samples (e.g., serum): Recommend -80°C long-term storage
Minimum Sample Submission Amounts
| Sample Type | Minimum Amount | Additional Requirements |
| Animal Tissue | 300 mg | Place in sterile tube, freeze rapidly, avoid freeze-thaw |
| Soft Tissue (leaves, flowers, etc.) | 300 mg | Same as above |
| Bacterial Cells | 500 mg | Concentrate by centrifugation before freezing |
| Fungal Cells | 8 g | Store dry or frozen |
| Cell Pellets | ≥ 8×107 cells | Concentrate by centrifugation, store at -80°C |
| Serum/Plasma | 1 mL | Sterile tube with appropriate anticoagulant or none |
| Urine | 50 mL | Add preservative or freeze for storage |
| Secreted Proteins (culture media, cerebrospinal fluid, etc.) | 10 mL | Place in sterile tube, freeze at -80°C |
Protein sulfenylation represents the dynamic process of cellular redox signaling and serves as a critical bridge for understanding the connection between oxidative stress and disease. Our integrated analysis service combines advanced mass spectrometry technology with deep proteomics expertise to provide researchers worldwide with accurate, reliable, and comprehensive modification analysis solutions. Whether you're conducting foundational research or applied development, we're committed to supporting your scientific goals through high-quality data and professional technical guidance to drive breakthrough discoveries in your research.
Reference
- Mu B, et al. Oxidative stress-mediated protein sulfenylation in human diseases: Past, present, and future. Redox Biol. 2024 Oct;76:103332.
