The NF-kappaB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IkappaB proteins. Most agents that activate NF-kappaB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IkappaB. The key regulatory step in this pathway involves activation of a high molecular weight IkappaB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKalpha and IKKbeta serve as the catalytic subunits of the kinase and IKKgamma serves as the regulatory subunit. Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKbeta (Ser176 and Ser180 in IKKalpha), which causes conformational changes, resulting in kinase activation.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2.
Application Dilute:
WB: 1:2000~1:5000 IF: 1:50~1:200
Application Notes:
IKKalpha/beta (Phospho-S180/181) polyclonal antibody detects endogenous levels of IKKalpha/beta protein only when phosphorylated at Ser180/181.
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