Overview

Protein glycosylation is one of the major post-translational modifications that can significantly impact protein folding, distribution, stability, conformation, and activity. Glycoprotein abundance, glycosylation degree, and glycan structure changes are closely related to many diseases (such as genetic diseases, immunodeficiency, cardiovascular diseases, and cancer). The research on glycoproteomics has become popular, increasing the demand for the development of quantitative glycomics strategies. These strategies need to be able to sensitively monitor the abundance and structural changes of glycans. The role and characteristics of glycans in biological systems can be clarified using these strategies.

In the past, people focused their research on the enrichment and separation of glycoproteins/glycopeptides, identification of glycosylation sites, and glycan structure analysis. So far, the development of quantitative glycomics has lagged slightly behind other studies. At present, a combination of multiple analytical techniques (such as capillary electrophoresis, liquid chromatography, and mass spectrometry) is mainly used to analyze glycoprotein quantitatively. To enhance the sensitivity in spectroscopy and mass spectrometry, it is necessary to label with ionic and/or hydrophobic reagents during the analysis. Labeling with stable isotope reagents has also been considered a feasible strategy to achieve relative quantification.

Fig.1 Quantitative proteomic schematic of serum glycoproteins. (Gao, 2015)

Accurate Glycoprotein Quantification to Facilitate Your Research

CD BioGlyco provides a variety of technologies for quantitative analysis of glycoproteins, mainly including fluorescence spectroscopy, capillary electrophoresis, laser-induced fluorescence detection, hydrophilic interaction chromatography with fluorophores, and mass spectrometry (MS). Our researchers provide the best experiment design according to our client's research needs.

Workflow

Applications

• Our glycoprotein quantification service can be used to identify abnormal glycosylation patterns in cancer, diabetes, neurodegenerative diseases, etc., and to discover potential biomarkers.
• Our glycoprotein quantification service can be used to analyze the function and activity of proteins, for example, to study the effect of glycosylation modifications on protein function.
• Our glycoprotein quantification service can be used to study glycosylation modifications in metabolomics.

Advantages of Us

• From sample preparation (protein extraction, digestion, glycoprotein/glycopeptide enrichment) to MS and bioinformatics analysis, our company provides a one-stop service.
• Our company uses high-throughput, high-sensitivity MS to analyze the small amount of raw samples required and relatively small experimental error.
• Our company not only provides experimental data but also offers to provide complete glycoproteomics information, including glycoprotein, locus, glycopeptide, glycoform, and biosignature analysis, to help clients interpret data.

Publication Data

Frequently Asked Questions

CD BioGlyco is a company with rich experience and a good reputation in the field of glycoproteomics. Our multi-platform methods and well-trained researchers will greatly accelerate our clients' research and help them explore glycobiology more comprehensively and accurately. If you are interested in our services, please contact us for more consultation and we will respond promptly.

Associated Services

We provide comprehensive N-glycosylation site occupancy and O-glycosylation site occupancy analysis services to help resolve the core features of protein glycosylation modifications. Through MS combined with a glycopeptide enrichment strategy, we precisely locate the modification sites of N-glycosylation and O-glycosylation in proteins, and quantitatively assess their site occupancy, revealing the efficiency of linking glycan and peptide chains as well as their heterogeneity.