In-plant cells, as in other eukaryotic cells, glycosylation usually occurs on secreted proteins, although some glycosylation reactions are also found on cytoplasmic and nuclear proteins. Glycosylation can be classified into N-glycosylation and O-glycosylation according to the way of connection between the oligosaccharide fraction and the protein backbone. Glycosylation modifications not only affect the spatial conformation, bioactivity, transport, and localization of proteins but also play a crucial role in specific biological processes such as molecular recognition, cellular communication, and signal transduction.

What We Offer

With the increasing resolution of mass spectrometry and the continuous development of bioinformatics, mass spectrometry has been widely used for glycosylation resolution, which usually uses enzymatic cleavage or chemical means to release glycopeptides from glycoproteins first, and then carries out the identification of glycosylation sites and the resolution of glycopeptide structures, respectively. However, there is no mature technique for the analysis of intact glycopeptides, but Lifeasible uses the HCD/ETD "dual fragmentation mode" of the new generation of combined mass spectrometry to resolve intact glycopeptides of complex glycoproteins and then uses Byonic software to analyze the raw mass spectrometry data. Lifeasible'glycosylated plant proteome analysis service provides large-scale identification of N-glycosylation and O-glycosylation modification sites/peptides/protein information in plant samples provided by customers, quantitative screening of N-glycosylation and O-glycosylation modification sites that are significantly differentially expressed between different groups of samples, analysis of the composition of the sugar chains carried by the corresponding sites, and bioinformatics analysis of the associated N-glycosylation and O-glycosylation modification proteins.

Service Flow

We Do Better

Lifeasible provides quantitative proteomic analysis of glycosylation. All you need to do is tell us your experimental objectives and send us your samples, and we will take care of all the follow-up of your project, including protein extraction, protein digestion, glycosylated peptide enrichment, peptide separation, mass spectrometry, raw data analysis by mass spectrometry, and bioinformatics analysis. Our service can detect up to tens of thousands of N-glycosylation modification sites at a time, which has the advantage of high identification throughput. Besides, we also provide combined glycoproteomics analysis.

Reference

1. Strasser R. “Plant protein glycosylation.” Glycobiology. 2016, 26(9):926-939.

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For research use only, not intended for any clinical use.

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