Characterization of five monoclonal antibodies raised against domain E of the porcine estradiol receptor.
Male Balb C mice were immunized with a pure 32 kDa fragment of the porcine estradiol receptor spanning the domain E. Five antibody-producing hybridoma lines were established from fusions of spleen cells with the myeloma lines SPO and NSO. The antibodies were analyzed for interaction with native and with denatured intact receptor and receptor fragments, respectively. The antigenic determinant for antibody 13H2 is a native epitope which retains its combining activity after receptor denaturation. The antibodies 1F5, 1G5, 3E6 and 2H10 react with denatured proteins only. The presence of the determinants of all five antibodies has also been demonstrated in human, bovine, rat and mouse estradiol receptor.
Thole
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HH
Max-Planck-Institut für experimentelle Endokrinologie, Hannover/Germany.
Jakob
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F
D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis* / Q000276:immunology; D000918:Antibody Specificity; D002417:Cattle; D000939:Epitopes / Q000276:immunology*; D006801:Humans; D006825:Hybridomas / Q000276:immunology; D008297:Male; D051379:Mice; D008807:Mice, Inbred BALB C; D010446:Peptide Fragments / Q000276:immunology; D011489:Protein Denaturation; D051381:Rats; D011959:Receptors, Estradiol / Q000276:immunology*; D013552:Swine
D000911:Antibodies, Monoclonal; D000939:Epitopes; D010446:Peptide Fragments; D011959:Receptors, Estradiol