Glycopeptide Enrichment Service
- Glycoprotein Biomarker Discovery: Enrich low-abundance glycopeptides from plasma, serum, or tissue to uncover disease-specific glycosylation changes.
- Biotherapeutic Characterization: Analyze glycosylation patterns of recombinant antibodies, fusion proteins, or glycoengineered biologics to support quality assessment and batch comparability.
- Cell Signaling and Immune Modulation: Investigate the glycosylation of receptors, adhesion molecules, and immune checkpoints to understand their regulatory mechanisms.
- Cancer and Inflammation Research: Explore glyco-signatures associated with tumor progression, metastasis, or chronic inflammation.
- Functional Proteomics and Multi-PTM Analysis: Integrate glycopeptide enrichment with phosphopeptide or acetylpeptide enrichment for multi-layered PTM studies.
- Avoid high salt, glycerol, or detergents like SDS
- Provide detailed buffer composition for compatibility check
- Snap freeze samples in liquid nitrogen and store them at -80℃
- Ship on dry ice with labeling and documentation
Protein glycosylation is one of the most abundant and functionally diverse post-translational modifications (PTMs) in eukaryotic organisms. Glycosylated proteins are involved in nearly every aspect of cellular function—including signal transduction, cell adhesion, immune modulation, protein folding, and degradation. However, due to the heterogeneity, low abundance, and substoichiometric nature of glycopeptides, they are often difficult to detect and quantify in standard proteomics workflows. Glycopeptide enrichment has become an essential preparative step to enable comprehensive glycoproteomic profiling by mass spectrometry (MS). Selective enrichment improves detection sensitivity, increases the dynamic range of glycopeptides, and ensures accurate site-specific characterization of glycan modifications. MtoZ Biolabs offers a high-efficiency Glycopeptide Enrichment Service to support accurate and in-depth glycoproteomic analysis.
Service at MtoZ Biolabs
MtoZ Biolabs' robust and flexible Glycopeptide Enrichment Service is designed to enhance the detection and profiling of glycosylated peptides in complex biological samples. The service enables selective enrichment of various types of glycopeptides, enhances MS signal-to-noise ratio, and support downstream qualitative or quantitative glycoproteomic analysis. Whether your goal is global glycoprotein profiling, biomarker discovery, or characterization of therapeutic glycoproteins, we provide end-to-end solutions—from sample preparation and enrichment protocol selection to LC-MS/MS analysis and data interpretation.
To meet diverse experimental goals and sample types, we implement multiple enrichment strategies based on distinct chemical properties of glycopeptides—such as hydrophilicity, glycan–lectin interactions, and covalent reactivity.
Glycopeptide Enrichment Methods Provided by MtoZ Biolabs:
💠Hydrophilic Interaction Liquid Chromatography (HILIC)
HILIC exploits the strong hydrophilicity of glycopeptides by retaining them on a polar stationary phase while non-glycosylated peptides are washed away. This approach is particularly suitable for N-linked glycoproteomics profiling.
💠Lectin Affinity Chromatography
Using lectins that bind specific glycan motifs, this method allows targeted enrichment of glycopeptides carrying defined carbohydrate structures, such as high-mannose, sialylated, or fucosylated glycans. It supports both N- and O-linked glycoproteomic analyses.
💠Hydrazide Chemistry (Solid-Phase Capture)
This method oxidizes sialic acid residues on glycopeptides to generate aldehyde groups, which covalently bind to hydrazide-functionalized beads. It enables selective enrichment of sialylated glycopeptides.
💠MOAC (Metal Oxide Affinity Chromatography)
MOAC utilizes metal oxides such as TiO₂ or ZrO₂, which interact with negatively charged moieties on glycopeptides, including sialic acids and phosphate groups. This method is well-suited for enriching acidic or sialylated glycopeptides from complex samples.
💠IMAC (Immobilized Metal Affinity Chromatography)
IMAC employs immobilized metal ions (e.g., Fe³⁺ or Ga³⁺) to capture glycopeptides bearing negatively charged groups, particularly sialylated structures. It is effective for selective enrichment of glycopeptides with anionic character.
Figure 1. Typical Glycoproteomics Workflow
Service Advantages
1. High Sensitivity and Specificity
Our optimized protocols enable efficient isolation of low-abundance glycopeptides from complex biological samples, ensuring high recovery rates and minimal background.
2. Customized Experimental Design
We design flexible, project-specific workflows to match your glycoproteomics objectives, whether for broad profiling or targeted analysis.
3. Integration with Advanced MS Analysis
Glycopeptide enrichment is seamlessly coupled with high-resolution mass spectrometry platforms, ensuring accurate glycosylation site identification and glycoform characterization.
4. Experienced Scientific Team
Our expert team brings years of hands-on experience in glycoproteomics and sample preparation, providing reliable technical support and data interpretation.
Applications
Our Glycopeptide Enrichment Service is applicable to a wide range of biological and translational research areas, including:
Sample Submission Suggestions
1. Buffer Requirements:
2. Storage and Transport:
*Note: If you have specific requirements or need guidance on sample preparation, please do not hesitate to contact us.
Deliverables
1. Comprehensive Experimental Details
2. Materials, Instruments, and Methods
3. Total Ion Chromatogram & Quality Control Assessment (project-dependent)
4. Data Analysis, Preprocessing, and Estimation (project-dependent)
5. Bioinformatics Analysis
6. Raw Data Files
Related Services
Peptide Enrichment Service | MS-compatible
Complete N-Glycopeptide Analysis Service
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