CHARACTERIZATION OF 5 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 por cine estradiol receptor spanning the domain E. Five antibody-producing hybridoma lines were established from fusions of spleen cells with th e myeloma lines SPO and NSO. The antibodies were analyzed for interact ion with native and with denatured intact receptor and receptor fragme nts, respectively. The antigenic determinant for antibody 13H2 is a na tive epitope which retains its combining activity after receptor denat uration. The antibodies 1F5, 1G5, 3E6 and 2H10 react with denatured pr oteins only. The presence of the determinants of all five antibodies h as also been demonstrated in human, bovine, rat and mouse estradiol re ceptor.