Activation of NFkB requires that IkB be phosphorylated on specific serine residues, which results in targeted degradation of IkB. IkB kinase alpha (IKKalpha), previously designated CHUK, interacts with IkB-alpha and specifically phosphorylates I°Balpha on Serine 32 and 36, the sites that trigger its degradation. IKKalpha appears to be critical for NFkB activation in response to proinflammatory cytokines. Phosphorylation of IkB by IKKalpha is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB 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 IkB 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:
WB: 1:1000~1:2000 IHC: 1:50~1:200 IF: 1:50~1:200
Application Notes:
IKKgamma (Phospho-S31) polyclonal antibody detects endogenous levels of IKKgamma protein only when phosphorylated at Ser31.
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