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Total cell lysates were collected at the indicated time points following cycloheximide treatment and subjected to immunoblot analysis with anti-HA antibodies. The amount of Nrf2 present at the beginning of cycloheximide treatment was set at 1. The half-life of Nrf2 in each group was indicated. Keap1-mediated nuclear export of Nrf2 is required for ubiquitination of Nrf2. The transfected cells were left untreated or treated with tBHQ for 4 h. Anti-Nrf2 immunoprecipitates IP were analyzed by immunoblotting with anti-HA antibodies for detection of ubiquitinated Nrf2 upper panel.

The chitin beads were pelleted and washed. Nuclear export of Nrf2 is required for repression of Nrf2-dependent transcriptional activity.

A plasmid encoding Renilla luciferase driven by the herpes simplex virus thymidine kinase promoter was included in all transfections to normalize transfection efficiency.

All samples were duplicated for each experiment, and the data shown represent the means for three independent experiments. The error bars indicate the standard deviations for the three experiments. Please note the difference in the scale of relative units between panels A and B. Nrf2, not Keap1, associates with ARE. Nuclear fractions were extracted and incubated with a 32 P-labeled ARE-containing oligonucleotide in the absence or presence of either the unlabeled competing oligonucleotides or antibodies.

The protein-DNA complexes were size separated on a nondenaturing polyacrylamide gel. The arrow indicates the position of the ARE-Nrf2 complexes. The asterisk indicates an ARE binding complex that does not contain Nrf2.

Two different types of Nrf2 antibodies were used. The one labeled with an asterisk has a higher concentration. DNA-protein complexes were cross-linked and immunoprecipitated with the indicated antibodies.

No Ab, no antibody. Nuclear import of Keap1 is independent of Nrf2. Subcellular localization of the indicated Keap1 protein was determined by an indirect immunofluorescence analysis using anti-CBD antibodies. B The same slides from panel A were used to count at least positive cells.

Keap1 confers postinduction repression of Nrf2 by escorting nuclear export of Nrf2. After removal of tBHQ by washing, cells were further incubated in normal medium for the indicated time periods. C Postinduction repression of the Nrf2-dependent transcriptional activity was determined in MDA-MB cells cotransfected with plasmids encoding an ARE-firefly luciferase, thymidine kinase- Renilla luciferase, Nrf2, and the indicated Keap1 protein.

Following removal of tBHQ, cells were further incubated in normal medium for the indicated time periods prior to measurement of firefly and Renilla luciferase activities. The experiment was repeated three times, and standard deviations are shown as error bars.

Schematic model of Nrf2 regulation by Keap1. Keap1 is a key regulator of the Nrf2 signaling pathway and serves as a molecular switch to turn on and off the Nrf2-mediated antioxidant response.

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HOOKUP SITE AUSSIE BABES DNA-protein complexes were cross-linked and immunoprecipitated with the indicated antibodies. The NES sequence with a cluster of hydrophobic residues is shown, and the four hydrophobic residues are replaced by alanines. C Postinduction repression of the Nrf2-dependent transcriptional activity was determined in MDA-MB cells cotransfected with plasmids encoding an ARE-firefly luciferase, thymidine kinase- Renilla luciferase, Nrf2, and the indicated Keap1 protein. At least positive cells were examined. Please note the difference in the scale of relative units between panels A and B.

Colocalization of the Nrf2 and Keap1 proteins is indicated by the presence of yellow in the merged images panels 4, 8, 12, 16, 20, 24, and D Subcellular localization of the Nrf2 and Keap1 proteins in double-transfected cells the same slides were used for C were examined and counted in the same way as in B except that the data were collected from cells that are positive for both Nrf2 and Keap1 proteins.

Nuclear and cytoplasmic proteins derived from equal numbers of cells were electrophoresed through a 7. B Subcellular distribution of Cul3, Nrf2, and Keap1 in singly transfected cells in the absence or presence of LMB was determined by indirect immunofluorescence staining.

At least positive cells were examined. Fifty micrograms per milliliter cycloheximide was added 36 h after transfection. Total cell lysates were collected at the indicated time points following cycloheximide treatment and subjected to immunoblot analysis with anti-HA antibodies. The amount of Nrf2 present at the beginning of cycloheximide treatment was set at 1.

The half-life of Nrf2 in each group was indicated. Keap1-mediated nuclear export of Nrf2 is required for ubiquitination of Nrf2. The transfected cells were left untreated or treated with tBHQ for 4 h. Anti-Nrf2 immunoprecipitates IP were analyzed by immunoblotting with anti-HA antibodies for detection of ubiquitinated Nrf2 upper panel. The chitin beads were pelleted and washed.

Nuclear export of Nrf2 is required for repression of Nrf2-dependent transcriptional activity. A plasmid encoding Renilla luciferase driven by the herpes simplex virus thymidine kinase promoter was included in all transfections to normalize transfection efficiency.

All samples were duplicated for each experiment, and the data shown represent the means for three independent experiments. The error bars indicate the standard deviations for the three experiments. Please note the difference in the scale of relative units between panels A and B. Nrf2, not Keap1, associates with ARE. Nuclear fractions were extracted and incubated with a 32 P-labeled ARE-containing oligonucleotide in the absence or presence of either the unlabeled competing oligonucleotides or antibodies.

The protein-DNA complexes were size separated on a nondenaturing polyacrylamide gel. The arrow indicates the position of the ARE-Nrf2 complexes.

The asterisk indicates an ARE binding complex that does not contain Nrf2. Two different types of Nrf2 antibodies were used. The one labeled with an asterisk has a higher concentration. DNA-protein complexes were cross-linked and immunoprecipitated with the indicated antibodies. No Ab, no antibody. Nuclear import of Keap1 is independent of Nrf2. Subcellular localization of the indicated Keap1 protein was determined by an indirect immunofluorescence analysis using anti-CBD antibodies.

B The same slides from panel A were used to count at least positive cells. Keap1 confers postinduction repression of Nrf2 by escorting nuclear export of Nrf2.

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This is something we encourage as it will enhance the experience for both of you. We would also appreciate your understanding if your booking is delayed a little because of an extension. We will always allow you the same opportunity. We always try to ensure the lady you have requested is available at the time you have booked however sometimes things are a little out of our control. If you make a booking and are unable to make it please let us know. This will assist us in providing a better service to you.

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