Figure 4
From: Fluorescent thermal shift-based method for detection of NF-κB binding to double-stranded DNA
Effect of withaferin A on the dsDNA-induced p65/RelA thermal stability shift. (a) Chemical structure of WFA. (b,c) The thermal denaturation of p651-306 was measured in the absence and presence of 10 µM 2κB dsDNA and varying concentrations of WFA, as indicated. Representative derivative (d(RFU)/dT) curves are shown for untreated and treated with 50 µM WFA samples. Midpoint temperatures of the protein-unfolding transition (Tm) are presented as bars. Values are mean ± SD of at least three separate measurements (***p < 0.001). (d) The inhibitory effect of WFA on the DNA-binding activity of p651-306 was verified by EMSA.
