Fig. 4.
Fig. 4. ICSBP and IRF-4/Pip form a complex in B cells and macrophages. (A) IRF-4/Pip is precipitated out of mouse B-lymphocyte extracts with an antibody against ICSBP. (A) Shows a mobility shift assay incubating the ISG15 ISRE oligonucleotide with wild-type mouse B-lymphocyte extracts, either mock-depleted (lanes 1 to 4) or depleted for the ICSBP protein (lanes 5 to 8). In lanes 2 and 6, the extracts are incubated with antibody against ICSBP, lanes 3 and 7 are with anti-IRF-4/Pip, and lanes 4 and 8 are with anti-IRF–2. (B and C) Evidence for ICSBP and IRF-4/Pip complex by coimmunoprecipitation in B-cell line, A20.2j (B) and in primary macrophages (C). The IRF-4/Pip protein was precipitated with an antibody against ICSBP and vice versa as described in Materials and Methods. Fluorographs of the immunoprecipitated fractions (P) and the supernatants (S) are shown.

ICSBP and IRF-4/Pip form a complex in B cells and macrophages. (A) IRF-4/Pip is precipitated out of mouse B-lymphocyte extracts with an antibody against ICSBP. (A) Shows a mobility shift assay incubating the ISG15 ISRE oligonucleotide with wild-type mouse B-lymphocyte extracts, either mock-depleted (lanes 1 to 4) or depleted for the ICSBP protein (lanes 5 to 8). In lanes 2 and 6, the extracts are incubated with antibody against ICSBP, lanes 3 and 7 are with anti-IRF-4/Pip, and lanes 4 and 8 are with anti-IRF–2. (B and C) Evidence for ICSBP and IRF-4/Pip complex by coimmunoprecipitation in B-cell line, A20.2j (B) and in primary macrophages (C). The IRF-4/Pip protein was precipitated with an antibody against ICSBP and vice versa as described in Materials and Methods. Fluorographs of the immunoprecipitated fractions (P) and the supernatants (S) are shown.

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