American Society of Hematology

Fig. 3.

$Fig. 3. Aberrant cellular localization and transcriptional activation by the mutant C/EBPε. / (A) Western blot analysis of whole cell lysates (lanes 1-3), cytoplasmic (C; lanes 4, 6, and 8), and nuclear (N; lanes 5, 7, and 9) fractions for C/EBPε and β-actin expression. The absence of the cytoplasmic protein β-actin in the nuclear fraction serves as a control for the experiment. The cells were transfected with expression vectors that were either empty (−) or encoded wild-type (W) or mutant (S) C/EBPε32 (32 and 24 kd, respectively). The arrows at the left of the panels indicate the positions of the proteins. (B) NIH3T3 cells were co-transfected with pG-CSFR-luciferase (firefly) and either empty (−), wild-type (WT), or mutant (SGD) C/EBPε32. Luciferase activity was measured and normalized to renilla luciferase used as a control for transfection efficiency. The experiment was performed twice in triplicate with results presented in relative light units (RLUs).$

Aberrant cellular localization and transcriptional activation by the mutant C/EBPε.

(A) Western blot analysis of whole cell lysates (lanes 1-3), cytoplasmic (C; lanes 4, 6, and 8), and nuclear (N; lanes 5, 7, and 9) fractions for C/EBPε and β-actin expression. The absence of the cytoplasmic protein β-actin in the nuclear fraction serves as a control for the experiment. The cells were transfected with expression vectors that were either empty (−) or encoded wild-type (W) or mutant (S) C/EBPε₃₂ (32 and 24 kd, respectively). The arrows at the left of the panels indicate the positions of the proteins. (B) NIH3T3 cells were co-transfected with pG-CSFR-luciferase (firefly) and either empty (−), wild-type (WT), or mutant (SGD) C/EBPε₃₂. Luciferase activity was measured and normalized to renilla luciferase used as a control for transfection efficiency. The experiment was performed twice in triplicate with results presented in relative light units (RLUs).

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