The transcription factor NFkappaB is retained in the cytoplasm in an inactive form by the inhibitory protein IkappaB. Activation of NFkappaB requires that IkappaB be phosphorylate on specific serine residues, which results in targeted degradation of IkappaB. IkappaB kinase alpha (IKKalpha), previously designated CHUK, interacts with IkappaB-alpha and specifically phosphorylates IkappaB-alpha on Serines 32 and 36, the sites that trigger its degradation. IKKalpha appears to be critical for NFkappaB activation in response to proinflammatory cytokines. Phosphorylation of IkappaB by IKKalpha is stimulated by the NFkappaB inducing kinase (NIK), which itself is a central regulato for NFkappaB activation in response to TNF and IL-1. The functional IKK complex contains three subunits, IKKalpha, IKKbeta and IKKgamma (also designated NEMO), and each appear to make essential contributions to IkappaB phosphorylation.
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:
IHC: 1:50~1:200
Application Notes:
p-IKKbeta (Y199) polyclonal antibody detects endogenous levels of IKKbeta protein only when phosphorylated at Tyr199.
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