IKKα, IKKβ, IKKγ, and IKKε antibodies detect endogenous levels of total IKKα, IKKβ, IKKγ and IKKε proteins, respectively. These antibodies do not cross-react with IKK subunits other than their specified target.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues at the carboxyl terminus of human IKKβ, IKKε and IKKγ, to the 20 amino-terminal residues of human IKKα. Antibodies are purified by protein A and peptide affinity chromatography.
Description
The IKK Isoform Antibody Sampler Kit provides an economical means to investigate NFkappaB signaling within the cell. 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).