Figure 1
(A) Schematic representation of the fusion proteins designed in the present study. The 6xHis tag was introduced for Ni-affinity chromatography. The MBP strongly enhances the solubility of the purified proteins. The cell-penetrating TAT motif was introduced at the C-terminus of MBP to allow the transport of the protein inside the cell. Two negative controls were utilized: One lacking the AICD domain, controlling for AICD independent effects, one lacking the TAT domain, precluding its entry into the cell and controlling for potential extracellular effects. (B) Coomassie stained gel of 1 μg of the purified proteins. Although a minor degradation product of the His–MBP–TAT–AICD protein is visible, most of the preparation represents the full length protein, indicated by the slightly higher apparent molecular mass compared with the control proteins His–MBP–TAT and His–MBP–TAT–AICD.
Construct design and purification of His–MBP–TAT, His–MBP–TAT–AICD and His–MBP–AICD

(A) Schematic representation of the fusion proteins designed in the present study. The 6xHis tag was introduced for Ni-affinity chromatography. The MBP strongly enhances the solubility of the purified proteins. The cell-penetrating TAT motif was introduced at the C-terminus of MBP to allow the transport of the protein inside the cell. Two negative controls were utilized: One lacking the AICD domain, controlling for AICD independent effects, one lacking the TAT domain, precluding its entry into the cell and controlling for potential extracellular effects. (B) Coomassie stained gel of 1 μg of the purified proteins. Although a minor degradation product of the His–MBP–TAT–AICD protein is visible, most of the preparation represents the full length protein, indicated by the slightly higher apparent molecular mass compared with the control proteins His–MBP–TAT and His–MBP–TAT–AICD.

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