Protein-protein interaction analysis of p53 and the α isoform of heat shock protein 90 (Hsp90α)

Abstract

<p><b>Copyright information:</b></p><p>Taken from "Proteomic identification of heat shock protein 90 as a candidate target for p53 mutation reactivation by PRIMA-1 in breast cancer cells"</p><p>Breast Cancer Research 2005;7(5):R765-R774.</p><p>Published online 27 Jul 2005</p><p>PMCID:PMC1242148.</p><p>Copyright © 2005 Rehman et al.; licensee BioMed Central Ltd.</p> MDA-231 cell lysates from untreated cells (lanes 1 and 3) and cells treated for 4 hours with 100 μM PRIMA-1 (lanes 2 and 4) were immunoprecipitated (IP) with anti-Hsp90α monoclonal antibody and subjected to Western blotting (WB) with anti-p53 (DO-1) monoclonal antibody (lanes 1 and 2) in addition to reciprocal immunoprecipitation with DO-1 and Western blotting with anti-Hsp90α (lanes 3 and 4). GI-101A cell lysates from untreated cells (lanes 1 and 3) and cells treated for 4 hours with 100 μM PRIMA-1 (lanes 2 and 4) were immunoprecipitated with anti-Hsp90α monoclonal antibody and subjected to Western blotting with anti-p53 (DO-1) monoclonal antibody (lanes 1 and 2) in addition to reciprocal immunoprecipitation with DO-1 and Western blotting with anti-Hsp90α (lanes 3 and 4)