IKKε/TBK1 Antibody

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 four proteins, IKKα, IKKβ, IKKγ, and IKKε. 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. IKKε has significant homology with IKKα and IKKβ. LPS increases IKKε mRNA level in mouse macrophages, and overexpression of wild type IKKε leads to phosphorylation of Ser-32 and Ser-36 of IκBα.

References

*For more information, see UniProt Accession Q9UHD2

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