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Catalog Antibody> | … For the His-tagged mouse FcγRIII, biotinylated anti-His IgG1 (GenScript, Piscataway, NJ, USA) was spotted in duplicate and three-fold dilution onto the sensor, ranging from 1 nM to 30 nM, and 100 nM mouse FcγRIII (equally diluted in PBS 0.075% Tween-80, pH 7.4) was … | Get A Quote |
The binding strength between IgG and FcγR is influenced by the composition of the N-linked glycan at position N297 in the Fc-domain of IgG. Particularly, afucosylation increases the binding affinity of human IgG1 to human FcγRIIIa up to ∼20 fold, and additional galactosylation of the afucosylated IgG increases the affinity up to ∼40 fold. The increase in affinity for afucosylated IgG has previously been shown to depend on direct carbohydrate-carbohydrate interactions between the IgG-Fc glycan with an N-linked glycan at position 162 unique to hFcγRIIIa and hFcγRIIIb. Here we report that the N162 glycosylation site is also found in the orthologous mouse FcγR, mFcγRIV. The N162-glycan in mFcγRIV w... More