The mutant leucine-zipper domain impairs both dimerization and suppressive function of Foxp3 in T cells -- Chae et al. 103 (25): 9631 Data Supplement - HTML Page - index.htslp -- Proceedings of the National Academy of Sciences

Chae et al. 10.1073/pnas.0600225103.

Supporting Figures

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Supporting Figure 7
Supporting Figure 8
Supporting Figure 9

Supporting Figure 7

Fig. 7. Each MSCV 2.2 encoding FLAG-tagged FoxP3 and FoxP3 (DE250) was transfected into 293T cells and cells were harvested after 48 h of transfection. Nuclear lysates were prepared and anti-FLAG mAb was used to probe Foxp3 expression. Anti-p38 was used as control to quantitate protein amount for each sample.

Supporting Figure 8

Fig. 8. FoxP3 and FoxP3 (DE250) protein levels in Jurkat cells and 293 cells corresponding to the conditions in Fig. 6. p38 was used as protein quantitation control by Western blot.

Supporting Figure 9

Fig. 9. FoxP3- and FoxP3DE-transfected Jurkat clones were pulsed with 1 mg/ml of doxycycline for 24 h. After 24-h induction, cells were washed with PBS extensively to remove residual doxycycline and incubated for 24, 48, 72, and 96 h in the absence of doxycycline. Nuclear lysates were prepared for each time point to monitor protein degradation. Western blot was performed with anti-FLAG mAb and p38 was used as a control for protein quantitation.