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Item No. 13923

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Explore how neutrophils shape the immune response in health and disease. This poster highlights neutrophil pathogen defense mechanisms, including phagocytosis, degranulation, and NETosis, as well as neutrophil roles in inflammation and NET-associated pathologies.
DOWNLOAD NOWIκBα 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 (Phospho-Ser32/36) Monoclonal Antibody (Clone 39A1413) can be used for immunoprecipitation (IP) and Western blot (WB) applications. The antibody recognizes IκBα (phospho-Ser32/36) from human, mouse, rat, porcine, bovine, and dog samples.
WARNING This product is not for human or veterinary use.
1. Regulation of IκBα function and NF-
2. Post-
3. Rel/NF-
4. Human IκBα gain of function: A severe and syndromic immunodeficiency. J. Clin. Immunol. 37(5), 397-412 (2017).