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. Author manuscript; available in PMC: 2013 Apr 1.
Published in final edited form as: Cancer Res. 2012 Feb 13;72(7):1740–1750. doi: 10.1158/0008-5472.CAN-11-2410

Fig. 1. Dmp1 co-immunoprecipitates with p53.

Fig. 1

(A), (B) NIH 3T3 cells were transfected with cDNA for FLAG-Dmp1, HA-p53, c-Myb, p19Arf, and/or Mdm2 expression vectors. The cleared lysates were immunoprecipitated with antibodies to (A) Dmp1 (FLAG) or (B) p53 (HA), and analyzed by Western blotting.

(C, left panels) Endogenous Dmp1-p53 interaction in U2OS cells treated with etoposide. Etoposide/MG-132 treated lysates were immunoprecipitated with control GFP antibody (sc-9996), control IgGs or antibodies to p53 (sc-126, sc-6243) or Dmp1 (RAD, RAX, RAZ), followed by blotting with Dmp1 or p53 antibodies.

(C, right panels) Endogenous Dmp1-p53 interaction in the mouse thymus injected with etoposide. Lysates were immunoprecipitated with control immunoglobulins, p53 antibody (sc-6243), or Dmp1 antibody (RAD) and analyzed by Western blotting.

(D) Recombinant FLAG-Dmp1, HA-p53, and FLAG-Mdm2 proteins were purified from baculovirus-infected Sf9 cells. In vitro binding assays were conducted by using 4 μg of proteins followed by immunoprecipitation with p53 (sc-6243), Dmp1 (RAX), or control IgGs, and analyzed by Western blottings.