Abstract
Objective To obtain monoclonal antibodies(McAb) against human IgE by recombinant IgE antigen.Methods BLAB/c mice were immunized with recombinant IgE.The spleen cells of immunized mice were used to prepare the McAb by hybridoma techniques.IgE-McAb was selected by indirect ELISA with culture supernatant of hybridoma cells.ELISA blocking assay were employed to identify the function of McAb.Alanine scanning mutagenesis were used to confirm the antigenic epitopes of McAb.Results A monoclonal antibody against IgE(178) was produced.The antigenic epitope of 178 was found to be spatially close to the receptor-binding site.Functional assay revealed that 178 could markedly inhibit IgE binding to receptors.Conclusion A hybridoma cell line secreting IgE-McAb stably was obtained by recombinant IgE antigen,and the IgE-McAb might block IgE binding to receptors via steric hindrance. Key words: Human IgE; Monoclonal antibody; Antigenic epitope
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