N-glycosylation is one of the most important protein post-translational modifications and is widely present in complex multicellular organisms. In this modification process, sugar chains are covalently attached to specific asparagine (Asn) residues on proteins (recognition sequence: N-X-S/T, where X cannot be proline). This modification primarily occurs in the endoplasmic reticulum and Golgi apparatus and involves multiple steps of sugar chain synthesis, transfer, and modification. Research indicates that approximately 50-70% of eukaryotic proteins undergo glycosylation modifications, making it the most prevalent post-translational modification in living organisms, with complexity far exceeding phosphorylation, ubiquitination, and other modification types.

N-glycosylation plays critical roles in various important life processes, including cell recognition and adhesion, receptor-ligand interactions, immune response regulation, protein stability and functional maintenance, apoptosis and metabolic regulation, and more. In particular, abnormal N-glycosylation is closely associated with pathological processes in cancer, neurodegenerative diseases, and immune disorders, making it an important research target for disease diagnosis, prognosis assessment, and development of novel therapeutic targets.

Our Services

We employ lectin enrichment combined with high-resolution mass spectrometry analysis to establish a comprehensive N-glycosylation proteomics service system:

1. High-Throughput Glycoprotein Proteomics Analysis

We utilize specific lectins to enrich N-glycosylated peptides and employ high-resolution mass spectrometry for site-specific and structure-specific analysis. This allows simultaneous detection of hundreds to thousands of glycosylation sites, enabling complete characterization of glycosylation profiles from individual sites to global proteome-wide patterns.

2. Multi-Condition Comparative Analysis

We perform systematic analysis of N-glycosylation proteomes under different experimental conditions (such as disease vs. normal states, pre- and post-drug treatment, time gradients, etc.) to identify critical glycosylation dynamic changes.

3. Signaling Pathway Integration Analysis

We correlate glycosylation changes with protein expression, phosphorylation, and other post-translational modifications to reveal key functional nodes of glycosylation in signaling pathways and establish relationships between glycosylation modifications and biological functions.

4. Candidate Glycoprotein Biomarker Screening

Using statistical methods and bioinformatics analysis, we screen for glycoproteins with diagnostic value, prognostic significance, or medication guidance potential from complex glycosylation data.

5. Quantitative Glycosylation Analysis

We support quantitative comparison of glycosylation levels between different samples and sites, providing robust statistical data support.

Service Advantages

Our analytical approach combines lectin multi-enrichment with high-resolution mass spectrometry detection, offering high sensitivity and specificity. By simultaneously acquiring peptide sequence information and glycan structure information while preserving the original site-glycoform correspondence, our method provides closer alignment with biological reality compared to simple glycan release analysis. The automated sample preparation workflow enables parallel processing of large sample batches, while rigorous quality control systems ensure data reproducibility and reliability. Our comprehensive bioinformatics analysis pipeline provides a solid foundation for subsequent biomarker validation and functional studies, supported by our experienced professional team offering customized analytical solutions and scientific guidance.

Workflow

Application

• Disease Research and Biomarker Discovery
  Early cancer detection, neurodegenerative disease research, autoimmune and immune disease diagnosis
• Drug Development and Quality Control
  Biopharmaceutical glycosylation characterization, batch-to-batch consistency assessment, biosimilar reference comparison
• Basic Research
  Glycosylation functional studies, condition-responsive analysis, glycosylation reprogramming during development and aging