Nitric oxide (NO) is an important intracellular signaling molecule that not only exerts biological effects through the cGMP signaling pathway, but can also regulate protein function through a parallel signal transduction pathway—S-nitrosylation modification. S-nitrosylation modification refers to the process where nitric oxide forms a covalent bond with the thiol group (-SH) of specific cysteine residues in proteins, creating a stable nitrosothiol structure. This modification is a reversible post-translational modification that not only alters the redox state of proteins, but more importantly enables:
These mechanisms make S-nitrosylation a critical regulatory point for cells to sense and respond to physiological and pathological stimuli.
Figure 1. Most relevant cysteine oxidation states in the context of S-nitrosylation and possible pathways of interconversion. (Source: Bignon E, et al. 2018)
| Service | Description | Key Components | Application Scenarios |
| S-Nitrosylation Proteome Profiling | Comprehensive and in-depth detection and quantification of S-nitrosylation sites in biological samples using advanced mass spectrometry technology |
|
Comprehensive understanding of protein modification landscape |
| Targeted Protein Nitrosylation Analysis | Precise detection of S-nitrosylation modification sites on specific proteins of interest |
|
Drug target validation, assessment of disease-related protein nitrosylation status |
| Comparative Condition Studies | Systematic comparison of S-nitrosylation modification patterns across different biological conditions |
|
Disease biomarker discovery, drug mechanism elucidation, stress response research |
| Multi-Modification Joint Analysis | Simultaneous detection of S-nitrosylation with other post-translational modifications such as phosphorylation and ubiquitination |
|
Complex signal pathway research, multi-target intervention strategy design |
We will record sample information and relevant experimental background, perform sample quality testing (including protein concentration and purity assessment), and develop a customized analysis plan based on the sample characteristics.
We perform protein extraction and quantification, protein reduction and alkylation treatment, as well as trypsin digestion to generate peptides, ensuring proper preparation for subsequent analysis.
We identify S-nitrosylation sites through specific chemical tagging, employ affinity chromatography to enrich modified peptides, and remove non-specific binding materials to enhance target abundance.
We conduct liquid chromatography-mass spectrometry (LC-MS/MS) analysis, acquiring high-resolution mass data and fragmentation spectra to ensure detection sensitivity and reproducibility.
We perform modification site identification and localization, qualitative and quantitative analysis of nitrosylated proteins, functional enrichment and pathway analysis, as well as statistical significance evaluation.
We generate a comprehensive technical report with interactive data visualization results, and offer optional in-depth biological interpretation and discussion.
| Sample Type | Recommended Amount |
| Conventional animal tissues (brain, heart, liver, kidney, etc.) | ≥300 mg |
| Soft tissues (plant leaves, flowers, etc.) | ≥300 mg |
| Bacterial cells | ≥500 mg |
| Fungal cells | ≥8 g |
| Cultured cells | ≥8×10⁷ cells |
| Sample Type | Recommended Amount |
| Serum/plasma | ≥1 mL |
| Urine | ≥50 mL |
| Other body fluids | ≥500 μL |
| Secreted proteins (cell culture supernatant, brain tissue secretion, etc.) | ≥10 mL |
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