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O-Glycosylation Site Occupancy Analysis

O-glycosylation of proteins is a common modification with diverse structures and functions. Due to the clinical and biopharmaceutical importance, it is necessary to comprehensively characterize O-glycoproteins including the determination of glycan composition, sequence and attachment site. Site-specific O-glycosylation analysis is key to explore structure-function relationships of glycoproteins, such as in the context of antigenicity and disease progression. Mass spectrometry (MS)-based methods have proven to be the core technique in site-specific O-glycosylation analysis.

Overview of O-Glycosylation Site Occupancy Analysis Service

Because the addition of O-glycans affects intracellular processes including protein folding and maturation, O-glycosylation site occupancy must be measured quantitatively to unravel the macroheterogeneity in glycoprotein populations, which is important for quality control of glycoproteins. Quantitation of O-glycosylation site occupancy can be applied to the fields of diagnostics, glycotherapeutics, and glycolengineering. At Creative Proteomics, we provide a reliable and affordable O-glycosylation site occupancy analysis service for academics, biotechnology, and pharmaceutical communities.

Mass spectrometry (MS) has emerged as a powerful tool for comprehensive analysis of glycoproteins. Creative Proteomics utilizes the most advanced MS platforms and other proteomic techniques to provide the accurate, reliable O-linked glycosylation site occupancy analysis service for identification of truly O-glycosylated peptides.

Protein digestion using enzymes.
O-Glycopeptide release through β-elimination.
O-glycopeptide enrichment using HILIC (hydrophilic interaction liquid chromatography).
Determination of O-linked glycosylation site occupancy using LC-ESI-MS/MS.

Sample Requirement

We work with a range of sample sources as follows.

Protein: 100 ug
Cells: 1×10⁷
Animal tissues: 1 g
Plant tissues: 200 mg
Anticoagulated blood (EDTA): 1 mL
Serum: 0.2-0.5 mL
Urine: 2 mL
Microbial sample: 200 mg (dry weight)

Advantages of O-Glycosylation Site Occupancy Analysis

High-sensitivity, reproducible quantification of rates of O-linked glycan site occupancy
Work with complex biological matrices, like cells and tissues
Comprehensive report containing raw data, parameters, data interpretation, and bioinformatics analysis

As one of the leading companies in the proteomics field with years of experience, Creative Proteomics provides glycomics analysis services that can be customized to your needs. Contact us to discuss your project.

Reference

Holland J W, Deeth H C, Alewood P F. Analysis of O‐glycosylation site occupancy in bovine κ‐casein glycoforms separated by two‐dimensional gel electrophoresis. Proteomics, 2005, 5(4): 990-1002.
Hoffmann M, Marx K, Reichl U, et al. Site-specific O-glycosylation analysis of human blood plasma proteins. Molecular & Cellular Proteomics, 2016, 15(2): 624-641.

* For Research Use Only. Not for use in diagnostic procedures.

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From Our Clients

"I recently used their proteomics service for a project analyzing protein interactions in yeast models. The team was very responsive and helped clarify the methodology they employed, which made me feel confident in the results. The data quality was solid, with clear identification of several key proteins involved in our study. Their thorough analysis enabled me to pinpoint specific interactions that I hadn't considered before, which significantly improved the direction of my research. I appreciate their professionalism and support throughout the process."

Sarah Thompson, University of California, Berkeley

"Our lab collaborated with them on a project studying cancer biomarkers. The proteomics analysis provided was detailed and focused, specifically highlighting the differential expression of proteins between healthy and tumor samples. Their clear explanations of the data helped my team understand the biological implications. I also appreciated their willingness to revise the reports based on our feedback, ensuring that we had everything we needed for our publication. This collaborative spirit was invaluable."

Emily Rodriguez, Stanford University

"Our lab worked with them on a project studying the effects of diet on gut microbiota using proteomics. They used a label-free quantification method to analyze proteins in fecal samples before and after dietary intervention. The results showed significant changes in protein expression linked to microbial activity. This was pivotal for our hypothesis about diet-microbiota interactions. The clarity of their data presentation made it easy for our team to integrate these findings into our ongoing research."

Dr. Lisa Wong, University of Toronto

"My experience with Creative Proteomics during the mass spectrometry analysis was excellent. We sent in human saliva and mouse brain tissue samples, which they expertly analyzed using both LC-MS and GC-MS techniques. The results were invaluable, revealing key metabolites in the saliva and identifying biomarkers linked to brain function in the brain tissue."

Dr. Emily Carter, Senior Research Scientist

"The overall service from Creative Proteomics was outstanding. They made the entire process seamless and efficient, allowing us to focus on our research. We worked with leaf and root samples from various Arabidopsis genotypes for targeted metabolomics analysis. Their thorough profiling of primary and secondary metabolites gave us important insights into how the plants respond metabolically to environmental stress."

Dr. Laura Henderson, Plant Physiologist

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