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. 2017 Jan 31;58(2):393–402. doi: 10.1194/jlr.M072447

Fig. 1.

Fig. 1.

LXRα binds fluorescently labeled saturated fatty acyl-CoA. A: Corrected fluorescence emission spectra of 0.1 μM LXRα titrated with 0 (filled circles), 2.5 (open circles), 5 (filled triangles), 10 (open triangles), 30 (filled squares), 50 (open squares), and 60 nM (filled diamonds) of BODIPY C12-CoA upon excitation at 465 nm, demonstrating that the enhanced fluorescence intensity of BODIPY C12:0-CoA is a result of direct binding with LXRα. B: Plot of LXRα maximal fluorescence emission as a function of BODIPY C12:0-CoA. C: Corrected fluorescence emission spectra of 0.1 μM LXRα titrated with 0 (filled circles), 5 (open circles), 10 (filled triangles), 30 (open triangles), 50 (filled squares), 90 (open squares), and 100 nM (filled diamonds) of BODIPY C16-CoA upon excitation at 465 nm demonstrating that the enhanced fluorescence intensity is a result of binding to LXRα. D: Plot of LXR maximal fluorescence emission as a function of BODIPY C16-CoA.