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.

Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.