N-Glycosylation Site Analysis Service | Biological Products

    N-glycosylation is a post-translational modification (PTM) involved in various physiological and pathological processes. The variability of glycosylation modification site is a key indicator of cellular activity, as evidenced by the correlation between the reduction of glycosylation attachment site on serum protein and the severity of congenital disorders of glycosylation (CDGs). Therefore, accurately determining site occupancy rate is crucial for understanding the impact of protein glycosylation on human health.

     

    To determine glycosylation attachment site, protein N-glycosidase F (PNGase F) is typically used in heavy water to separate polysaccharides from proteins. During this process, the originally glycosylated asparagine undergoes deamidation to become aspartic acid, with an addition of an O18 modification. Because the introduction of O18 changes the molecular weight, glycosylation sites can be detected by comparing peptides containing aspartic acid with those containing unglycosylated asparagine. The general strategy for analyzing variable N-glycosylation site in glycoproteins includes protein digestion with PNGase F, polysaccharide release, separation of glycopeptide by liquid chromatography (LC), and detection by mass spectrometry (MS).

     

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

     

    Deliverables

    1. Experimental Procedures

    2. Mass Spectrometric Parameters

    3. Mass Spectrometric Images

    4. Raw Data

    5. Detailed Information on Identified Glycosylation Sites

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