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Figure S1: 2D Western blots for phospho-serine 15 and phospho-serine 392 of p53 in whole lysates of Raji cells treated with 2-FaraA (3 μM) for control, 24 h and 48 h treated samples. Serine 15 is phosphorylated in control and 2-FaraA treated cells, and remains phosphorylated in the low molecular weight derivatives. Full length p53 is phosphorylated at Serine 392 after treatment with 2-FaraA, but not in control cultures. However, treatment of 2-FaraA does not induce phosphorylation of low molecular weight derivatives at Serine 392. Extracts (100 μg protein) were focused on an 11 cm pH 3-10 IPG strip and separated in the second dimension using 4-12% SDS-PAGE. Proteins were then transferred onto a PVDF membrane and Western blotting was performed with the p53 antibodies (#9284S) and (#9281S).

Figure S2: 2D Western blots for p53 in whole lysates of Raji cells treated with 2-FaraA (3 μM ) ± the pan caspase inhibitor Z-VAD-FMK (100 μM) for control, 24 h and 48 h treated samples. Western blotting is described in Materials and Methods. A p53 derivative of 25 kDa is indicated by an arrow for 2-FaraA-treated cells without Z-VAD-FMK.

Figure S3: 1D Western blots for p53 family members in whole lysates of different cell lines treated with 2-FaraA (3 μM). Cells were harvested and lysed in Laemmli buffer. Changes in protein levels can be compared with changes in mRNA levels in Figure 8.

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