Glycan Standards & Libraries
AdvanceBio 2-AA Human α-1-acid glycoprotein N-glycan library (formerly ProZyme). Library is derived from α-1-acid glycoprotein, which is heavily glycosylated (~45% carbohydrates) and contains five N-glycosylation sites. The Human α1-Acid glycoprotein N-linked glycan library represents a total pool of N-linked glycans released from Human α1-acid glycoprotein. These glycans constitute a heterogenous mixture of core non-fucosylated bi-, tri- and tetraantennary glycans with various degrees of sialylation (NeuAc) and some with outer arm fucose residues and lactosamine repeats, consistent with N-glycans previously reported for human α1-acid glycoprotein. The biantennary glycans can have one or two sialic acid residues. The triantennary and tetraantennary glycans can have from one to four sialic acid residues and may be substituted with fucose, resulting in formation of sialyl Lewis X like structure.
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