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.
Fig.1 Glycomics/glycoproteomics workflow for the analysis of a purified glycoprotein. (Yang, 2017)
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.
Reference