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. 2002 May;76(10):4928–4939. doi: 10.1128/JVI.76.10.4928-4939.2002

FIG. 3.

FIG. 3.

Association of v-Rel dimerization mutants with Rel/NF-κB proteins. v-Rel proteins were cotranslated in an in vitro system with truncated v-Rel proteins (v-RelΔ), c-Rel (aa 1 to 284), NF-κB1 (p50), and NF-κB2 (p52) in the presence of [35S]methionine. All cotranslations contained approximately equal amounts of each protein. Translated products were directly analyzed by SDS-PAGE (first four lanes) or were subjected to immunoprecipitation with an antiserum specific to the C terminus of v-Rel and then resolved by SDS-PAGE (last four lanes). Proteins were visualized by phosphorimager analysis. The identity of the v-Rel protein studied is indicated to the right of each panel. The Rel/NF-κB proteins present in each reaction are indicated on the top of each panel.