Establishment of hybridomas secreting monoclonal antibodies against C epsilon 2 and C epsilon 4 domains of human IgE.
Three kinds of hybridomas secreting monoclonal antibodies (MAbs) against the epsilon chain of human IgE were constructed by somatic cell hybridization between mouse myeloma P3U1 cells and spleen cells from BALB/c mice immunized with human IgE purified from the culture supernatant of U-266 cells. These MAbs were used effectively for the purification and determination of human IgE. The recognition site in the IgE molecule of each antibody was examined by using various epsilon chain fragment peptides produced in Escherichia coli. From these experiments, it was suggested that one recognized C epsilon 2 and the second C epsilon 4. The third did not recognize the C epsilon 1-C epsilon 4 domains of the recombinant epsilon chain from E. coli, although it bound to the epsilon chain of natural human IgE.
Ichimori
Y
Y
Kurokawa
T
T
Ikeyama
S
S
Sasada
R
R
Tsukamoto
K
K
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000939:Epitopes; D006825:Hybridomas; D007127:Immunoglobulin Constant Regions / Q000276:immunology*; D007143:Immunoglobulin Heavy Chains / Q000276:immunology*; D007139:Immunoglobulin epsilon-Chains / Q000276:immunology*; D007136:Immunoglobulins / Q000276:immunology*; D051379:Mice; D008807:Mice, Inbred BALB C
D000911:Antibodies, Monoclonal; D000939:Epitopes; D007127:Immunoglobulin Constant Regions; D007143:Immunoglobulin Heavy Chains; D007139:Immunoglobulin epsilon-Chains; D007136:Immunoglobulins