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Gene Regulation

Phospho-IκBα / NFκB Translocation

phosphorylation of IκBα leads to the activation of NFκB

NFκB proteins are among the most widely studied transcription factors because they have been shown to regulate a variety of genes that control inflammation, cell proliferation and cell survival. In addition, aberrant activity of NFκB has been observed in many human cancers.

In unstimulated cells, NFκB dimers are sequestered in an inactive state in the cytoplasm by the IκB family of inhibitor proteins, which mask the nuclear localization signals of the NFκB proteins. The best-studied IκB protein is IκBα. In response to a variety of external stimuli, human IκBα is phosphorylated at Ser32 & Ser36 by IκB Kinase (IKK) proteins. This results in the ubiquitination, dissociation from NFκB and degradation of IκBα. The newly "freed" NFκB complex can then translocate to the nucleus where it regulates gene expression through DNA binding (see Diagram below).

Active Motif's FunctionELISA™ IκBα is ideal for studying IκBα phosphorylation, while the TransAM®, LightSwitch™ and Luminex® product lines are for the study of NFκB.

Diagram of IkBa phosphorylation which leads to NFkB translocation & activation
Diagram of IκB phosphorylation and NFκB translocation/activation.