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. 2011 Feb 17;6(2):e17206. doi: 10.1371/journal.pone.0017206

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Cattaneo 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. SEL1LA and p28 immunoprecipitation analysis: Left panel: SKBr3 cell lysates (1.4 mg) were immunoprecipitated with monoclonal anti-SEL1L antibody (lane 3), resolved by SDS-PAGE (10%) and probed with monoclonal anti-SEL1L antibody. Lysate aliquots (50 µg, lane 1) were loaded to verify protein expression levels and immunoprecipitation efficiency. Arrows indicate the immunoprecipitated bands, asterisks (*) correspond to heavy and light chains. Absence of signal in controls (lanes 4 and 5) confirms the specificity of the immunoprecipitated bands. Right panel: SKBr3 cell lysates (7.0 mg) were immunoprecipitated with monoclonal anti-SEL1L antibody (lane 4), resolved by SDS-PAGE (10%) and stained with Coomassie brilliant blue. Asterisks (*) correspond to heavy and light chains. The arrow indicates the immunoprecipitated band analyzed by mass spectrometry. Absence of signal in controls (lanes 1 and 3) confirms the specificity of the immunoprecipitated band. B. Analysis of the interaction between SEL1L variants and TPD52: Left panel: SKBr3 cell lysates (1.4 mg) were immunoprecipitated with monoclonal anti-SEL1L antibody (lane 3), resolved by SDS-PAGE (10%) and probed with polyclonal anti-TPD52 antibody. Lysate aliquots (40 µg, lane 4) were loaded to verify protein expression levels and immunoprecipitation efficiency. Lane 5 corresponds to unbound aliquots of the samples loaded in lane 4 (40 µg). The arrow indicates the immunoprecipitated band. Absence of signal in controls (lanes 1 and 2) confirms immunoprecipitation specificity. Right panel: SKBr3 lysates (1.4 mg) were immunoprecipitated with polyclonal anti-TPD52 antibody (lane 3), resolved by SDS-PAGE (10%) and probed with monoclonal anti-SEL1L antibody. Lysate aliquots (40 µg, lane 4) were loaded to verify protein expression levels and immunoprecipitation efficiency. Lane 5 corresponds to unbound aliquots of the samples loaded in lane 3 (40 µg). The membrane was successively re-probed with anti-TPD52 antibody. Arrows indicate the immunoprecipitated bands. Absence of signal in controls (lanes 1 and 2) confirms immunoprecipitation specificity.