Purified proteins were used to coat 96-well plates (30 ng/well) overnight at 4°C. Culture supernatants from individual hybridomas were added to each well (100 µl/well) followed by horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG (Novus). The values of the optical density (OD) of substrate reactions were read at 450 nm on a plate reader (Bio-Rad).
The binding ability of mAb was measured by ELISA as described previously [31 (link),32 (link)]. MAbs were serially two-fold diluted at an initial concentration of 10 µg/ml and detected by ELISA as described above.
The binding ability of mAb was measured by ELISA as described previously [31 (link),32 (link)]. MAbs were serially two-fold diluted at an initial concentration of 10 µg/ml and detected by ELISA as described above.
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