Nuclear Factor-κB (NF-κB) is sequestered in the cytoplasm by the 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 result in phosphorylation and degradation of IκB, releasing NF-κB dimers. NF-κB dimers subsequently translocate to the nucleus and activate target genes. Synthesis of IκBα is autoregulated. IκB proteins are phosphorylated by IκB kinase complex consisting of at least three proteins, IKK1/α, IKK2/β, and IKK3/γ. IKKγ preferentially interacts with IKKβ and is required for activation of IKK complex. IKKγ is also known as NF-κB essential modulator (NEMO). The human T-cell leukemia virus type I Tax oncoprotein that activates NF-κB binds neither to IKKα nor IKKβ, but complexes directly with IKKγ. This suggests that IKKγ may be a key molecule acting as an adapter for oncoprotein specific signaling to IKKα and IKKβ.

• Starting concentration for WB is 2 µg/ml
• For immunochemical analysis of IKKγ

Type: Primary
Antigen: His-tagged IKK-gamma
Clonality: Monoclonal
Clone: 72C627
Conjugation: unconjugated
Epitope: Full length
Host: Mouse
Isotype: IgG
Reactivity: Human, Mouse