IκBα (human, recombinant)

IκBα is an inhibitor of NF-κB and a member of the IκB family of proteins.^1,2,3 It is composed of an N-terminal signal-receiving domain, which contains several post-translational modification sites that regulate its activity, an ankyrin-repeat domain, which contains six ankyrin repeats that mediate protein-protein interactions with NF-κB dimers, a proline-glutamic acid-serine-threonine (PEST) domain, and two nuclear export sequences.² IκBα is ubiquitously expressed and shuttles between the cytoplasm and nucleus.^1,2,3 IκBα is phosphorylated by the IκB kinase (IKK) complex, which is activated via downstream signaling events stimulated by TNF-α, other cytokines, viruses, or bacteria, and its phosphorylation leads to its ubiquitination and degradation by the proteasome. The degradation of IκBα results in unmasking of the nuclear localization signal of NF-κB dimers, which subsequently translocate to the nucleus and activate target genes. Mutations in NFKBIA, the gene encoding IκBα, are associated with anhidrotic ectodermal dysplasia with immunodeficiency.⁴ Cayman’s IκBα (human, recombinant) protein consists of 323 amino acids and has a calculated molecular weight of 36.4 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 38 kDa.

WARNING This product is not for human or veterinary use.

1. Majdalawieh, A., and Ro, H.-S. Regulation of IκBα function and NF-κB signaling: AEBP1 is a novel proinflammatory mediator in macrophages. Mediators Inflamm. 823821 (2010).

2. Wang, X., Peng, H., Huang, Y., et al. Post-translational modifications of IκBα: The state of the art. Front. Cell Dev. Biol. 8, 574706 (2020).

3. Verma, I.M., Stevenson, J.K., Schwarz, E.M., et al. Rel/NF-κB/IκB family: Intimate tales of association and dissociation. Genes Dev. 9(22), 2723-2735 (1995).

4. Boisson, B., Puel, A., Picard, C., et al. Human IκBα gain of function: A severe and syndromic immunodeficiency. J. Clin. Immunol. 37(5), 397-412 (2017).