Glycoproteomics Platform
Glycosylation is present on 50% of proteins and is considered an important post-translational modification. Protein glycosylation plays a key role in many biological processes, such as cell adhesion, protein translation regulation, cellular immunity, protein degradation, etc. The glycosylation pattern changes during tumor development, which can be used for early cancer diagnosis and monitoring the progress of tumorous diseases. Glycoproteomics is a branch of proteomics used to identify, classify, quantify, and characterize glycoproteins, which includes the elucidation of glycosylation sites and the analysis of glycoprotein structure and function.
The comprehensive analysis of glycoproteins is particularly challenging due to the structural diversity of glycans and the heterogeneity of glycosylation sites. In recent years, the rapid development of mass spectrometry (MS) instruments, fragmentation strategies, and high-throughput workflows has made it possible to analyze intact glycoproteins. Several enrichment methods can detect even low abundances of glycans and glycopeptides, and various experimental workflows tailored for the quantification, site occupancy and structural analysis of glycoproteins have been developed, resulting in the rapid development of glycoproteomics.
To overcome the challenge of glycoprotein analysis, CD BioGlyco provides a variety of enrichment and purification methods to improve the detection sensitivity. We provide fast and efficient glycoprotein enrichment services, such as O-Glycoprotein and Peptide Enrichment.
CD BioGlyco offers a diverse range of cutting-edge technologies tailored for the quantitative analysis of glycoproteins, encompassing fluorescence spectroscopy, capillary electrophoresis, laser-induced fluorescence detection, hydrophilic interaction chromatography coupled with fluorophore labeling, and MS. Our team of seasoned researchers meticulously crafts optimized experimental designs to align precisely with the unique research requirements of our clients. We specialize in delivering comprehensive solutions for both relative and absolute quantitative analyses of glycoproteins, ensuring precision and reliability in every study.
The properties of glycoproteins are largely affected by site occupation. To further study the microheterogeneity of glycoproteins, we provide site occupancy analysis.
We use advanced technologies such as MALDI-TOF and HILIC to analyze the complex structure of glycoproteins and their derivatives.
Our lab provides professional SARS-CoV-2 Glycosylation Profiling to accelerate your project research. We provide the most comprehensive glycomics analysis to systematically analyze the coronavirus-related glycoproteins of interest to clients, including glycosylation profiling, comparative characterization (changes in the propagation process and the comparison with the glycosylation characteristics of SARS-COV, etc.).
CD BioGlyco's professional research team is deeply engaged in the field of N-glycoproteomics analysis of PDX models. It deeply analyzes structural variations and functional associations of glycoproteins through high-precision glycosylation profiling and dynamic monitoring technologies.
CD BioGlyco integrates several nanotechnologies for the detection of glycopeptides in complex samples with high sensitivity and specificity.
CD BioGlyco has deep technical accumulation and rich practical experience in glycan biomarker research. We integrate traditional glycomics methods (e.g., MS, lectin microarrays) with cutting-edge single-molecule detection technologies (e.g., nanopore sensing, AI-assisted signaling) to achieve precise capture and dynamic monitoring of ultra-trace glycan biomarkers in serum, extracellular vesicles, tissue sections, and other types of biological samples.
Technology: MS, Tandem MS (MS/MS)
Journal: Cells
Published: 2024
IF: 5.1
Results: This review summarizes the applications and advances of MS in O-glycoproteomics. The development of MS strategies has significantly advanced the study of O-glycoproteomics, especially in terms of sample preparation, enrichment strategies, and MS/MS techniques. Bottom-Up (BU) MS is performed by enzymatically cleaving proteins into peptides and utilizing MS/MS to identify peptide sequences, modification sites, and glycan chain composition. This method is suitable for the analysis of complex samples. Top-Down MS directly analyzes intact proteins, retaining combinatorial information on modifications, and is suitable for resolving post-translational modifications (PTMs) patterns of proteins.
Fig.1
Comparison of MS methods for resolving proteins. (Helms & Brodbelt, 2024)
CD BioGlyco has rich experience in glycoproteomics analysis. Our well-trained researchers provide a variety of high-quality analysis services according to your research needs. We hope to start the exploration of glycobiology with you. If you are interested in our services, please contact us for more detailed information.
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