Figure 1
Figure 1. In vitro binding activity of 3G8 scFv-HSA for huFcγRIIIA. Binding of 3G8 scFv-HSA fusion protein to the soluble domain of huFcγRIIIA was assessed by ELISA. A high-binding plate was coated with recombinant huFcγRIIIA overnight. (A) To detect direct binding of 3G8 scFv-HSA to huFcγRIIIA, scFv-HSA or HSA (highest concentration: 870 nM) was added, and bound 3G8 scFv-HSA was detected by anti-HSA-HRP. n = 6 replicates; data representative of 3 independent experiments. (B) To assess the ability of 3G8 scFv-HSA to competitively inhibit huIgG binding to huFcγRIIIA, various concentrations of 3G8 scFv-HSA (highest concentration: 650 nM), HSA (highest concentration: 650 nM), 3G8 (highest concentration: 67 nM), or vehicle were added to wells containing 0.8 µg/mL huIgG. n = 4 replicates; data representative of 5 independent experiments. All data points represented as mean ± standard error of the mean.

In vitro binding activity of 3G8 scFv-HSA for huFcγRIIIA. Binding of 3G8 scFv-HSA fusion protein to the soluble domain of huFcγRIIIA was assessed by ELISA. A high-binding plate was coated with recombinant huFcγRIIIA overnight. (A) To detect direct binding of 3G8 scFv-HSA to huFcγRIIIA, scFv-HSA or HSA (highest concentration: 870 nM) was added, and bound 3G8 scFv-HSA was detected by anti-HSA-HRP. n = 6 replicates; data representative of 3 independent experiments. (B) To assess the ability of 3G8 scFv-HSA to competitively inhibit huIgG binding to huFcγRIIIA, various concentrations of 3G8 scFv-HSA (highest concentration: 650 nM), HSA (highest concentration: 650 nM), 3G8 (highest concentration: 67 nM), or vehicle were added to wells containing 0.8 µg/mL huIgG. n = 4 replicates; data representative of 5 independent experiments. All data points represented as mean ± standard error of the mean.

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