Supplementary Figure 1: Quantitation of the binding of pro53 peptide to sorLA Vps10p measured by the AP reporter assay. | Nature Structural & Molecular Biology

Supplementary Figure 1: Quantitation of the binding of pro53 peptide to sorLA Vps10p measured by the AP reporter assay.

From: Structural basis for amyloidogenic peptide recognition by sorLA

Supplementary Figure 1

The graph shows tracings of the typical chromogenic AP reaction observed with AP-pro53 (orange) or control AP-MycHis (blue) eluted from the sorLA Vps10p-beads. Note that gradual increase in the absorbance with the AP-MycHis is indistinguishable from that with mock sample (where no AP activity is present in the reaction mixture), indicating that the background nonspecific binding of AP protein to the beads is negligible.

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