Isolation of IgG and glycan analysis has been described in detail in previous studies. An example protocol and details about each study can be found in the Supplementary Note. Briefly, IgG was first isolated using affinity chromatography binding to protein G plates, followed by release and labeling of glycans with 2-AB (2-aminobenzamide) fluorescent dye. Glycans were then separated and quantified by hydrophilic interaction UPLC, resulting in 24 chromatographic peaks. Most of the peaks contain a single glycan structure, while some contain more than one, but with at least 63% of the peak being contributed by the most abundant glycan (36).

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