Phospho-IKKα/β (Ser176/180) Antibody, Phospho-IKKα/β (Ser176/180) Antibody II, and Phospho-IKKα/β (Ser176/180) (16A6) Rabbit mAb detect IKKα only when phosphorylated at Ser176/180 and IKKβ only when phosphorylated at Ser177/181.
Source / Purification
Polyclonal antibodies #2687 and #2694 are produced by immunizing rabbits with a synthetic phosphopeptide corresponding to residues surrounding Ser176/180 of human IKKα and Ser177/181 of IKKβ, respectively, and are purified by protein A and peptide affinity chromatography. Monoclonal antibody #2697 is produced by immunizing rabbits with a synthetic phosphopeptide corresponding to residues surrounding Ser176/180 of human IKKα.
Description
The Phospho-IKKalpha/beta (Ser176/180) Antibody Sampler Kit contains reagents to examine protein levels of IKKalpha when phosphorylated at Ser176/180 and IKKbeta when phosphorylated at Ser177/181. The kit contains primary and secondary antibodies to perform four Western blots with each antibody.
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).