N-terminal Glycosylation of Protein
Glycosylation of proteins refers to the process where sugar chains are attached to proteins through glycosidic bonds, catalyzed by glycosyltransferases, reacting with active groups of amino acid side chains in peptide chains. N-terminal protein glycosylation involves the covalent attachment of a sugar chain containing 14 monosaccharides (Glc-3-Man-9-GlcNAc-2) to the amide group of asparagine (Asn) on the protein in the form of an N-glycosidic bond, transferring the sugar chain from a dolichol phosphate carrier to the protein.
Since N-glycosyltransferase can only recognize specific amino acid sequences Asn-X-Thr/Ser (X can be any amino acid except proline) for modification, the sequence of the N-terminal protein glycosylation site has site specificity. Additionally, the N-glycosylation sugar chain has a pentasaccharide core structure region, composed of 2 N-acetylglucosamine and 3 mannose, which can be further modified with other sugars to form complex N-glycan structures.
Biotech company Biotech-Peak uses high-resolution mass spectrometry system MALDI TOF MS and UHPLC technology to provideN-glycan analysisservices, which can be used to identify all N-glycans expressed in plasma/serum, cells, tissues, or organisms. All glycans attached to proteins are enzymatically digested and hydrolyzed, separated by hydrophilic chromatography, and quantitatively analyzed using the MALDI-TOF MS system. You simply need to inform us of your experimental objectives and send in your samples, and we will handle all subsequent project matters, including protein extraction, proteolysis, peptide separation, mass spectrometry analysis, raw data analysis, and bioinformatics analysis.
Related services:
N-glycosylation and modification sites
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