Phospho-IKKα/β (Ser176/180) Antibody II detects endogenous levels of IKKα and IKKβ only when phosphorylated at Ser176 and Ser180 or Ser177 and Ser181, respectively.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a phosphopeptide corresponding to a region surrounding Ser177/181 of IKKβ. Antibodies are purified by protein A and peptide affinity chromatography.
Background
The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex, whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation; Ser177 and Ser181 in the activation loop of IKKβ (serine 176 and 180 in IKKα) are the specific sites whose phosphorylation causes conformational changes resulting in kinase activation (10-13).