Relative Quantification of Glycoprotein
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)
Our company provides relative quantification of glycoproteins, which is designed to provide insight into how complex glycosylation modifications affect protein function, disease states, and the properties of biopharmaceuticals. We utilize advanced MS to enable precise comparisons of glycoproteins in different samples, providing clients with multi-dimensional information on glycosylation.
Relative quantification of Glycoprotein at the Site Specific Glycosylation Level
This service focuses on comparing the relative abundance of the same glycoprotein with a specific glycan structure in different samples. Our service can be used to analyze whether the level of a specific type of N-glycan or O-glycan (e.g., hypersalivation, fucosylation, altered branching, etc.) modification is increasing or decreasing on a key glycoprotein.
Relative quantification of Glycoprotein at the Protein Level
Research teams of CD BioGlyco have applied advanced techniques in proteomics to the study of glycoproteins, successfully achieving relative quantification of glycoproteins at the protein level. We provide relative quantitative analysis of glycosylation modifications as well as glycoprotein core protein abundance.
Relative quantification of Glycoprotein at the Glycosylation Occupancy Level
CD BioGlyco has established multiple methods for rapid and accurate relative quantification of glycoproteins at the glycosylation occupancy level, providing customers with technical support in studying glycoproteins' functions. This service is designed to quantify the presence or absence of glycosylation at a particular glycosylation site and the relative change in the extent or frequency with which the site is modified by glycosylation.
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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