Glycosylation, one of the most common and diverse post-translational modifications (PTMs), impacts a wide variety of cellular mechanisms, including protein stability, activity and folding. Glycosylated proteins, also known as glycoproteins, are found ubiquitously in eukaryotic organisms. Protein glycosylation includes the covalent attachment of carbohydrate groups to amino acids, ranging from simple monosaccharides to complex polysaccharides. There are several different types of glycosylation, including N-linked glycosylation, O-linked glycosylation, C-linked glycosylation and glypiation. N-linked glycosylation, the most common glycosidic linkage, is named as such because the glycans are bound to nitrogen residues or asparagine residues. N-linked glycosylation often occurs co-translationally, meaning that the glycan is attached to the lysine residue as it is being translated and transported into the Endoplasmic Reticulum (ER). Unlike N-linked glycosylation, O-linked glycosylation does not occur co-translationally, but post-translationally on serine and threonine residues in the Golgi apparatus. C-linked glycosylation, often referred to as C-mannosylation, is a reaction that forms C-C bonds, instead of C-O or C-N bonds. Last but not least, glypiation is a covalent attachment of a GPI anchor which results in the recruitment of proteins to cell membranes.
Glycosylation Bioinformatics Tool
Laverne is a handy bioinformatics tool to help facilitate scientific exploration of related genes, diseases and pathways based on co-citations. Explore more on Glycosylation below!
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We have 7045 products for the study of Glycosylation that can be applied to Flow Cytometry, Western Blot, Immunocytochemistry/Immunofluorescence, Immunohistochemistry from our catalog of antibodies and ELISA kits.