We have prepared a monoclonal antibody, KJ16-133, from the cells of a rat immunized with the purified receptor for antigen plus I-A of a BALB/c T cell hybridoma, DO-11.10. Unlike most other monoclonal anti- receptor antibodies that have been described before, KJ16-133 is not clone specific. It reacts with approximately 20% of the receptors on T cells of normal BALB/c mice. It also reacts with about the same percentage of antigen-specific, major histocompatibility complex (MHC)- restricted or allogeneic I-region specific T cell hybridomas. Reaction of KJ16-133 with a given T cell hybridoma does not seem to depend on the antigen specificity or MHC-restricting element of the T cell in question. The determinant recognized by KJ16-133 has some unexpected properties. It is absent in several strains of mice including SJL/J and SJA/20, but present on the T cells of most other commonly used strains. The determinant recognized therefore does not map to Igh. Our experiments suggest that a clone-specific "antiidiotypic" antibody and KJ16-133 recognize determinants on different parts of the receptor. For example, the binding of a clone-specific antibody to target T cells is relatively temperature insensitive, whereas KJ16-133 binds well to cells at 37 degrees C but poorly to cells at 4 degrees C. The determinant recognized by a clone-specific antibody is sensitive to reduction and alkylation of the receptor, whereas KJ16-133 reactivity is not. Finally, binding of KJ16-133 at saturating concentrations to target T cells does not block the binding of a clone-specific antibody. Similarly, binding of a clone-specific antibody only marginally inhibits binding of KJ16-133. Taken together, these results suggest that KJ16-133 is directed against an allelic determinant on T cells that may be close to the membrane, and not in the receptor binding site for antigen plus MHC. The antibody may recognize an allele of a constant region isotype, or an allele of a J region.