Six hybridomas secreting monoclonal antibodies that are specific for t
he N-terminal peptide sequence of the murine Ah receptor were isolated
, These antibodies bind with high specificity to the Ah receptor on pr
otein blots of Hepa 1c1c7 cytosol. Three IgG(1) antibodies (Rpt 1, 2,
and 3) were capable of detecting 2 ng of receptor using peroxidase-goa
t anti-mouse IgG antibody conjugate on a protein blot. Monoclonal anti
body Rpt 9 exhibited the greatest ability to immunoprecipitate the non
denatured 9S form of the Ah receptor and to visualize the AhR on liver
tissue sections using immunohistochemical techniques, All of the mono
clonal antibodies produced were able to bind to the mouse, rat, and hu
man Ah receptor. These monoclonal antibodies should be useful in a wid
e number of applications in the study of Ah receptor biochemistry.