Co-IP shows capture of UN2A by S100A1. Purified UN2A and S100A1 were incubated together, and the S100A1 was precipitated using an α-S100A1 antibody. Samples were separated by SDS-PAGE and analyzed by silver-staining. Lanes 1 and 3 are controls of the individual proteins showing that the antibody captures the S100A1 but not the UN2A. The presence of the UN2A along with the S100A1 in lane 2 supports our hypothesis that the S100A1 and UN2A interact with S100A1 is in the Ca2+-bound state. The contrast and brightness of the original image was adjusted slightly to improve the signal to noise between the gel and the bands. Source data are available for this figure: SourceData F3.
Figure 3.

Co-IP shows capture of UN2A by S100A1. Purified UN2A and S100A1 were incubated together, and the S100A1 was precipitated using an α-S100A1 antibody. Samples were separated by SDS-PAGE and analyzed by silver-staining. Lanes 1 and 3 are controls of the individual proteins showing that the antibody captures the S100A1 but not the UN2A. The presence of the UN2A along with the S100A1 in lane 2 supports our hypothesis that the S100A1 and UN2A interact with S100A1 is in the Ca2+-bound state. The contrast and brightness of the original image was adjusted slightly to improve the signal to noise between the gel and the bands. Source data are available for this figure: SourceData F3.

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