Glycosylated Peptides Analysis Service
- Accurately detects low-abundance glycopeptides for reliable results.
- Provides detailed glycan structure analysis to support drug development.
- Precisely identifies glycosylation sites to optimize drug efficacy.
- Accurately quantifies glycosylation efficiency to ensure product quality.
Glycosylation is a common post-translational modification (PTM) of proteins, which significantly affects the function and stability of proteins. Glycosylated peptides refer to the form in which glycan chains are attached to peptide segments, encompassing information on the amino acids of the peptides, complete glycan chains information, and the binding sites of glycan chains and peptides. Glycosylated peptide analysis is a widely applied technology in fields such as protein function regulation, drug development, bioengineering, and biopharmaceuticals. Analyzing glycosylated peptides provides detailed information about the quality, charge state, connection locations, and glycan chain structures of glycosylated peptides, which is also crucial for understanding the mechanisms of glycosylation regulation.
MtoZ Biolabs has developed a comprehensive glycosylation analysis method for specific glycoproteins based on a high-resolution mass spectrometry platform that combines liquid chromatography, providing you with high-quality one-stop glycosylated peptide analysis services, accurately analyzing types of glycosylation modifications, glycosylation site modification efficiency, and the proportion of various glycan types at glycosylation sites. Free project evaluation，Welcome to learn more details!
Analysis Workflow
Figure 1. Workflow for Glycosylated Peptides Analysis
Experimental Instruments
1. NanoLC: Vanquish NEO
2. MS: Orbitrap Fusion Lumos With ETD
Service Advantages
Applications
The analysis of glycosylated peptides can achieve comprehensive glycosylation analysis of specific glycoproteins, with information including:
1. The positioning of glycosylation sites, i.e., which sites in the protein have undergone glycosylation modification.
2. Differentiating between N-glycosylation sites and O-glycosylation sites to determine the type of glycan chains modification.
3. Obtaining the glycan chains composition, structure, and relative content information for each N-glycosylation site.
4. Obtaining the glycan chains composition and relative content information for each O-glycosylation site.
Statistical summaries of the above information can further analyze and explain the glycosylation characteristics of glycoproteins.
Case Study
1. Types of Glycosylation Modifications
Figure 2. Types of Glycosylation Modifications Statistics
*Type: Type of glycosylation modification; Position: Position of the glycosylation site in the protein; Glycans NHFAGNa: Type of glycan chains in the modification; Modification Type(s): Molecular weight of the glycan; Score: Protein scoring value; Intensity: Relative abundance of the protein; Percentage %: The proportion of this glycan type at each respective site among all glycan types.
2. Glycosylation Site Modification Efficiency
Figure 3. Glycosylation Efficiency Statistics
*Glycosylation efficiency (%) = (sum of relative contents of peptides with glycosylation at the same site / sum of relative contents of peptides without glycosylation at the same site) × 100
3. Proportion of Various Glycan Types at Each Glycosylation Site
Figure 4. Glycan Type Proportion
*The figure shows the N-glycan types and proportions at a specific site, with the horizontal axis representing the glycan type and the vertical axis indicating the proportion of the glycan types.
4. Summary Diagram of Protein Glycosylation Modification Information
Figure 5. Glycosylation Information Summary Diagram
*The figure shows the top three glycan contents at each site.
Deliverables
MtoZ Biolabs will provide you with a detailed technical report, including:
1. Experimental Procedures
2. Relevant Mass Spectrometry Parameters
3. Detailed Information on Glycosylated Peptide Analysis
4. Mass Spectrometry Images
5. Raw Data
How to order?
