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 phosphorylated on specific serine residues, which results in targeted degradation of IkappaB. IkappaB kinase alpha (IKKalpha), previously designated CHUK, interacts with IkB-a and specifically phosphorylates IkappaB-alpha on the sites that trigger its degradation, serines 32 and 36. The functional IKK complex contains three subunits, IKKalpha, IKKbeta and IKKgamma (also designated NEMO), and each appear to make essential contributions to IkappaB phosphorylation. TANK binding kinase (TBK1), also designated T2K, is a novel IKK-related kinase that has been identified in murine and human tissues. TBK1 was shown to complex with TRAF2 and TANK in the NFkappaB activation pathway. TBK1 shares homology with IKKalpha and IKKbeta in the amino-terminal half, which includes the kinase domain.
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:1:500~1:1000
Application Notes:
TBK1 (Phospho-S172) polyclonal antibody detects endogenous levels of TBK1 protein only when phosphorylated at Ser172.
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