Validation of Phospho-IkBα (Ser32/36)(12C2) Monoclonal Antibody in a peptide DELFIA® assay, using biotinylated phospho-, nonphospho-peptide controls, and DELFIA® secondary antibodies (available from PerkinElmer Life and Analytical Sciences).
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Phospho-IκBα (Ser32/36) (12C2) Monoclonal Antibody can be used in high throughput kinase assays and drug discovery applications. It detects peptides derived from IκBα phosphorylated at Ser32/36.
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser32/36 of human IκBα. Antibody is purified by protein G chromatography.
The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins (1-3). Activation occurs via phosphorylation of IκBα at Ser32 and Ser36 followed by proteasome-mediated degradation that results in the release and nuclear translocation of active NF-κB (3-7). IκBα phosphorylation and resulting Rel-dependent transcription are activated by a highly diverse group of extracellular signals including inflammatory cytokines, growth factors, and chemokines. Kinases that phosphorylate IκB at these activating sites have been identified (8).
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