Glycosylation is a type of post-translational modification (PTM) of proteins with high abundance and particularly complex structural types. It is estimated that more than 50% of the proteins expressed by cells are glycoproteins. The abundant and diverse glycoproteins play important roles in intracellular and intercellular processes such as signal transduction, immune regulation, and protein stability maintenance. With the development of enrichment methods, MS technologies, and spectral interpretation approaches for intact glycopeptides, comprehensive and systematic glycoproteomics analysis has greatly expanded the knowledge of protein glycosylation. Creative Proteomics is dedicated to helping our customers to achieve their goals, including glycosylation site identification, glycoprotein/glycan quantification, glycan sequence/structure detection, and so on.
Mass spectrometry-based method for identification of glycopeptides
Biological mass spectrometry (MS) is the most commonly used tool for glycoproteomics analysis. Mass spectrometric analysis of intact glycopeptides has begun to yield abundant glycopeptide fragment ions and abundant high-quality mass spectrometric data. Common techniques include matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS) and liquid chromatography-tandem mass spectrometry (LC-MS/MS), etc. And common MS fragmentation modes include collision-induced dissociation (CID), high-energy collision dissociation (HCD), electron transfer dissociation (ETD), etc. In addition to MS fragmentation, MS data acquisition modes, such as data-dependent acquisition (DDA), data-independent acquisition (DIA), multiple reaction monitoring technology (MRM), parallel reaction monitoring technology (PRM), etc., have great potential for application in glycoproteomics. For example, ETD and HCD coupled MS fragmentation technique can effectively improve the identification throughput, coverage depth and site designation accuracy of the O-glycan proteome.
Our glycoproteomics analysis capability
Since the low abundance of many glycoproteins and the tremendous structural diversity of glycans, it is extraordinarily challenging to explore specific functions of glycosylation. Our platform combines glycopeptide/glycoprotein enrichment strategies with advanced and effective MS-based methods. We can help our customers with the following lists:
- Isolation of complex glycoproteins or of numerous glycoproteins encountered in complex biological samples, including cells, tissues, physiological fluids, and microorganisms.
- Globally analyze glycoproteins and detect glycosylation sites.
- Systematically quantify glycoprotein and related glycoprotein dynamics.
- Selectively characterize glycoproteins with particular glycans.
Discover our specific services
Service features
- Powerful mass spectrometric analysis.
- Provide detailed reports, including relevant MS parameters, raw data, details of identified glycosylation sites, mass spectrometric images, etc.
- Provide a variety of bioinformatics analysis.
- One-stop service: Sample processing - Mass spectrometric analysis - Bioinformatics analysis - Project report.
Application of our service
- Study of glycosylation modification patterns of disease-related proteins.
- Antibody-drug quality evaluation, such as monoclonal antibody (mAb) drugs.
- Disease biomarker screening.
- Drug targets for disease treatment.
- Virus glycosylation research.
Creative Proteomics focuses on post-translational modification (PTM) proteomics analysis. Our platform is dedicated to developing and optimizing protein and peptide enrichment protocols and MS assays for a wide range of animal, plant, and microbial samples, and can provide technical support for the entire process of experiment design, sample pre-processing, on-board testing, data quality control, and bioinformatics analysis. If you are interested in our glycoproteomics analysis service, please feel free to contact us.
References
- Xiao, Haopeng, et al. "Mass spectrometry-based chemical and enzymatic methods for global analysis of protein glycosylation." Accounts of chemical research 51.8 (2018): 1796-1806.
- Xiao, Haopeng, et al. "Global and site-specific analysis of protein glycosylation in complex biological systems with Mass Spectrometry." Mass spectrometry reviews 38.4-5 (2019): 356-379.
- Duivelshof, Bastiaan L., et al. "Glycosylation of biosimilars: Recent advances in analytical characterization and clinical implications." Analytica chimica acta 1089 (2019): 1-18.
Our products and services are for research use only.
