Protein glycosylation, the most common post-translational modification process in eukaryotic cells, plays a crucial role in the correct biological function of proteins. Studies have shown that many diseases are accompanied by abnormal changes in the structure and expression of glycan chains on the intracellular glycoprotein. The detection of abnormal expression of glycoprotein chains can be used as a signal of cellular pathology. Therefore, glycans can be used as biomarkers for the diagnosis of certain diseases.
To understand the roles of glycoproteins in numerous disease mechanisms that depend on glycan-protein binding, it is critical to quantify glycoproteins at the site-specific glycosylation level, protein level, and glycosylation occupancy level. At present, the relative quantitative and qualitative analysis of glycan samples from different sources can be carried out by the combination of isotope labeling and modern biological mass spectrometry techniques, to investigate whether and how differently glycan chains are expressed in different samples. In addition, several effective strategies have been described for glycoprotein quantification, such as lectin microarrays, liquid chromatography-mass spectrometry (LC-MS), normal-phase high-performance liquid chromatography (HPLC), and multiple reaction monitoring (MRM).
Fig.1 Quantitative measurements of N-linked glycoproteins by SRM or SWATH-MS. (Liu, 2013)
Relative quantification of glycoprotein has been recognized as an important method for analyzing the physiological state or pathological status of cells. CD BioGlyco has completed many glycoprotein quantification cases. As a biotechnology company in the field of glycobiology, we expect to revolutionize your project and contribute to your success. If you have special requirements, please contact us for further information. We will do our best to provide you with the optimal service.
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