Fig. 3
Binding of BAZ to PDI protein in live HT22 cells in culture. A, B. Surface plasmon resonance analysis of the binding affinity of BAZ for the purified wild-type PDI-His256 protein (A for the concentration-dependent binding curve; B for Scatchard plot analysis based on the data in A). C. CETSA analysis of the change in PDI thermostability in 10 μM BAZ-treated intact cells in response to increasing temperatures (n = 3). D. ITDRCETSA analysis of the change in PDI thermostability in intact cells at 59 °C in the presence of increasing concentrations of BAZ. E. Relative intensities of the protein bands in panel C after quantified using the Image J software. For CETSA curves, the relative band intensities are calculated according to the intensities at the lowest temperature for the BAZ-exposed samples and control samples, respectively (n = 3). F. Relative intensities of the protein bands in panel D after normalized to the β-actin samples (n = 3). Quantitative data are presented as mean ± S.D. (** P < 0.01)