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Electrophoretic mobility gel shift assay was performed to determine the nuclear binding activity of nuclear factor κ-B (NFκB).
Furthermore, MEIO inhibited the LPS-induced DNA binding activity of nuclear factor-κB (NF-κB), and this was associated with the prevention of inhibitor κB degradation and a reduction in nuclear p65 protein levels.
Thereafter, whether EAW can enhance binding activity of nuclear Nrf2 to the ARE was evaluated.
DNA binding activity of nuclear factor (NF)- κB was evaluated using an enzyme-linked immunosorbent assay method.
Furthermore, the increased DNA binding activity of nuclear proteins from A-172/neo or A-172/mp53/248 cell was suppressed by wortmannin (Fig. 3, lane 5).
In addition, DNA binding activity of nuclear NF-κB p65, as demonstrated by highly sensitive and specific ELISA, was also inhibited in OA chondrocytes.
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The DNA-binding activity of nuclear factor κB (NFκB) and activator protein 1 (AP-1) components was measured by ELISA-based assays.
AP-1-binding activity of nuclear extracts produced from PCM rats was reduced by the presence of anti-c-Jun antibody.
Mechanistically, HDACIs increased prostratin-induced DNA-binding activity of nuclear NF-κB and degradation of cytoplasmic NF-κB inhibitor, IκBα.
Mechanistically, HDACis increased prostratin-induced DNA-binding activity of nuclear NF-κB and degradation of cytoplasmic NF-κB inhibitor, IκBα.
However, HNE inhibited the phosphorylation of IκBα and subsequently the DNA-binding activity of nuclear factor-κB.
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