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hae12072-sup-0001-FigureS1.tiffTIFF image2702KFigure S1. Restoration of diminished mutant rFXIII-As by a proteasome inhibitor. BHK cells expressing rFXIII-As were cultured in the presence (+) or absence (−) of 25 μm MG-132, a potent inhibitor of proteasome activity. rFXIII-As (red) and a proteasome marker, proteasome 20S core subunit (green), inside BHK cells were visualized by immune staining using an anti-FXIII-A or anti-proteasome 20S core subunit antibody. Only wild-type rFXIII-A (WT; top) was abundant in the cytoplasm, while R260C (middle) and Del-IV (bottom) mutants were barely seen, in the absence of MG-132. All rFXIII-As were clearly demonstrated to colocalize with proteasome 20S core subunit in the presence of MG-132, indicating the rapid degradation of mutants in the proteasome in the absence of MG-132.

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