Fig. 7.
Fig. 7. GILZ physically associate in vitro with p65 and p52. / GST-GILZ fusion protein attached to glutathione Sepharose beads was incubated with 35S-labeled in vitro–transcribed p65, p52, c-fos, and Fra-1. Lanes 1, 4, 7, 10: in vitro–translated proteins (2 μL); lanes 2, 5, 8, and 11: in vitro–translated proteins (5 μL) precipitated by the GST-GILZ fusion protein attached to glutathione beads; lanes 3, 6, 9, 12: in vitro–translated proteins after precipitation with GST protein attached to glutathione beads.

GILZ physically associate in vitro with p65 and p52.

GST-GILZ fusion protein attached to glutathione Sepharose beads was incubated with 35S-labeled in vitro–transcribed p65, p52, c-fos, and Fra-1. Lanes 1, 4, 7, 10: in vitro–translated proteins (2 μL); lanes 2, 5, 8, and 11: in vitro–translated proteins (5 μL) precipitated by the GST-GILZ fusion protein attached to glutathione beads; lanes 3, 6, 9, 12: in vitro–translated proteins after precipitation with GST protein attached to glutathione beads.

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