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. Author manuscript; available in PMC: 2011 May 1.
Published in final edited form as: Biochim Biophys Acta. 2010 Feb 16;1803(5):591–597. doi: 10.1016/j.bbamcr.2010.02.003

Figure 2. Examination of the interactions between epitope-tagged LRBP and prey proteins in vitro.

Figure 2

(A) List of proteins synthesized with [35S]-Methionine in vitro. Proteins expressed in pGBKT7 plasmids (LRBP and p53) are Myc tagged.

(B) Proteins were in vitro synthesized in the presence of 35S-methionine. Freshly synthesized LRBP and UBCE2i were mixed together and coimmunoprecipitated with anti-Myc antibody (lane4). The precipitated complex was analyzed by SDS-PAGE and autoradiography. Immunoprecipitation was specific (lane5, LRBP only) and no cross reaction was observed (lane6, UBCE2i only). The p53-SV40 interaction was used as a positive control (lane 1-3). Position of each protein ladder band was marked on the film.

(C) Proteins were in vitro synthesized in the presence of 35S-methionine. LRBP and RP S20 were coimmunoprecipitated with anti-Myc antibody (lane1) and analyzed by SDS-PAGE and autoradiography. Immunoprecipitation was specific (lane2, LRBP only) and no cross reaction was observed (lane3, RPS20 only). Position of each protein ladder band was marked on the film.