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tra12162-sup-0001-FigureS1.jpgJPEG image245KFigure S1. Detection of Hyal-1 by zymography in the liver of wild-type or Hyal-1 deficient mice. An ML fraction was prepared from the liver of the two types of mice and analyzed for Hyal-1 activity by ‘renatured protein zymography’ or ‘native protein zymography’.
tra12162-sup-0002-FigureS2.jpgJPEG image482KFigure S2. Distribution of control enzymes in the PercollTM gradient fractions of Figure 4C. The distributions of β-galactosidase, alkaline α-glucosidase and the refractive indexes are shown.
tra12162-sup-0003-FigureS3.jpgJPEG image54KFigure S3. Analysis of the glycosylation pattern of rhHyal-1. The recombinant protein was treated with endo H or PNGase F for 2 h at 37°C, then resolved by SDS-PAGE and visualized by western blotting.
tra12162-sup-0004-FigureS4.jpgJPEG image80KFigure S4. Validation of the 1D10 anti-Hyal-1 antibody for western blotting experiments in macrophage cells. Bone marrow monocytes were isolated from wild-type or Hyal-1 deficient mice, cultured in the presence of M-CSF for 4 days to induce differentiation into macrophages, then lysed and analyzed by western blotting with the 1D10 antibody.

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