NF-κB (nuclear factor κB) is sequestered in the cytoplasm by IκB family of inhibitory proteins that mask the nuclear localization signal of NF-κB thereby preventing translocation of NF-κB to the nucleus. External stimuli such as tumor necrosis factor or other cytokines results in phosphorylation and degradation of IκB releasing NF-κB dimers. NF-κB dimer subsequently translocates to the nucleus and activates target genes. Synthesis of IκBα is autoregulated. IκB proteins are phosphorylated by IκB kinase complex consisting of at least three proteins, IKKα, IKKβ, and IKKγ. IKKα and IKKβ are phosphorylated by NF-κB-inducing kinase (NIK) and MAP kinase kinase kinase-1 (MEKK1), respectively. Recent studies have shown that IKKβ, not IKKα, is the target of proinflammatory stimuli. Targeted disruption of IKKβ gene in mice also results in extensive liver damage from apotopsis and death during embryo development.
Hu, Y. et al. (1999) Science 284:316.
Takada, K. et al. (1999) Science 284:313.
Delhase, M. et al. (1999) Science 284:309.
*For more information, see UniProt Accession O15111
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains: