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. 2011 Sep 1;6(9):e23906. doi: 10.1371/journal.pone.0023906

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Sidera et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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A. Left panel: SDS-PAGE of purified antibodies under reducing conditions followed by Coomasie Brilliant Blue-R staining revealed in all cases an approximately 25 kDa band corresponding to the L-chain. Right panel: Under non-reducing conditions the antibodies are shown to migrate as a L-chain dimer. B. Western blot of MDA-MB-453 cell lysates using mAb 4C5, rec-4C5, ch-4C5 and a commercial anti-HSP90α antibody, serving as positive control. In all cases a single 90 kDa immunoreactive band corresponding to HSP90 is observed. C. Immunoprecipitation in MDA-MB-453 cell lysates with anti-HSP90α, followed by immunoblotting with either the murine or the recombinant antibodies. In all cases a single immunoreactive band is observed. D. Reverse immunoprecipitation experiments in MDA-MB-453 cell lysates using mAb 4C5, rec-4C5 and ch-4C5, followed by western blot with anti-HSP90α. In all cases a single immunoreactive band is observed indicating that both recombinant antibodies recognize HSP90.