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Studies on the human basophil IgE receptor. Generation and characterization of monoclonal antibodies against the
Anti-human basophil IgE receptor (Fc epsilon R) monoclonal antibodies (McAbs) were generated and characterized. The production of these antibodies was facilitated by both a single step procedure for the enrichment of basophils using Ficoll-Paque centrifugation and a double staining technique combining the APAAP with alcian blue. By the double staining technique we could recognize the specific anti-basophil antibodies because the cells binding the antibody--APAAP positive cells--also had alcian blue-stained basophil granules. Blocking experiments showed that the McAb was directed against the Fc epsilon R since preincubation with human IgE blocked the binding of the McAb and preincubation with the antibody blocked the binding of IgE to basophils and inhibited the formation of IgE rosettes.
Anti-human basophil IgE receptor (Fc epsilon R) monoclonal antibodies (McAbs) were generated and characterized. The production of these antibodies was facilitated by both a single step procedure for the enrichment of basophils using Ficoll-Paque centrifugation and a double staining technique combining the APAAP with alcian blue. By the double staining technique we could recognize the specific anti-basophil antibodies because the cells binding the antibody--APAAP positive cells--also had alcian blue-stained basophil granules. Blocking experiments showed that the McAb was directed against the Fc epsilon R since preincubation with human IgE blocked the binding of the McAb and preincubation with the antibody blocked the binding of IgE to basophils and inhibited the formation of IgE rosettes.