p-IKK? (S31) polyclonal antibody detects endogenous levels of IKK? protein only when phosphorylated at Ser31.
Activation of NFkB requires that IkB be phosphorylated on specific serine residues, which results in targeted degradation of IkB. IkB kinase ? (IKK?), previously designated CHUK, interacts with IkB-? and specifically phosphorylates I?B? on Serine 32 and 36, the sites that trigger its degradation. IKK? appears to be critical for NFkB activation in response to proinflammatory cytokines. Phosphorylation of IkB by IKK? 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, IKK?, IKK? and IKK? (also designated NEMO), and each appear to make essential contributions to IkB phosphorylation.
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