O-Glycan Profiling Service

    Glycosylation analysis is one of the most challenging types of post-translational modification (PTM) analysis. Glycosylation modifications typically occur at the group level rather than as individual modifications. Even a single glycosylation site on a protein may exhibit various chain lengths and multiple polysaccharide isomers with different branching. O-glycosylation (also referred to as O-Glycan or O-oligosaccharide) primarily forms through a linkage of glycosidic bond between the terminal monosaccharide residue and the hydroxyl group of either serine or threonine to the peptide. The common amino acid sequence linked by O-glycans is not yet clear, and the structure of O-glycans is diverse, which can be categorized into several families with relatively heterogeneous core structures.


    Unlike N-glycans, there is currently no common enzyme that can digest most O-glycans. O-glycoproteases can only enzymatically cleave oligosaccharides released by unsubstituted O-GalNAc disaccharides. Therefore, chemical hydrolysis of O-oligosaccharides is a more common method, through which most O-oligosaccharides can be released from O-glycopeptides, named as β-elimination.


    MALDI-TOF-MS can be used to analyze O-oligosaccharides. Methylating O-oligosaccharides by derivatization to convert all hydroxyl groups into methyl ether groups and stabilizing sialic acids by esterification the carboxyl groups can analyze O-glycans by MALDI-TOF-MS in positive mode. Analysis of methylated O-glycans by MS provides information about the composition of the polysaccharides.


    MtoZ Biolabs has much analytical service experience in glycomics and can customize glycomics analysis services according to your specific needs. Free consultation is available!



    1. Experimental Procedures

    2. Mass Spectrometry Parameters

    3. Mass Spectrometry Images

    4. Raw Data

    5. O-Glycan Profiling Results

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