di-sialylated core 2 O glycan, C2S(3,3)2, 2-AA Labelled [O-Glycan Standards] (CAT#: CB-P384-K) Datasheet

Glycan Standards

O-glycosylation is a common covalent modification of serine and threonine residues in mammalian glycoproteins. The most common type of O-glycosylation found on secreted mammalian glycoproteins and mucins (proteins bound to carbohydrates) is the addition of N-acylgalactosamine (GalNac) to serine or threonine residues. The core 1 structure was produced by adding galactose b1-3 to this GalNAc. The Core 2 structure is generated by further adding N-acetylglucosamine b1-6 to the N-acetyl-galactosamine on the Core 1 structure. A total of eight different core structures have been identified, and all of these core structures can be further extended by adding many monosaccharides including sialic acid. These O-glycans are found in biological drugs such as erythropoietin (EPO), etanercept (Enbrel) and human coagulation factor VIII (FVIII). Core 1 and Core 2 O-glycans are also found in biopharmaceuticals, such as erythropoietin (EPO), etanercept (Enbrel), human clotting factor VIII (FVIII), clotting factor IX and insulin glargine.