NFKBIA Research Reagents

NF-kappa-B inhibitor alpha is a protein in humans that is encoded by NFKBIA gene. Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and proinflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription.

The following NFKBIA reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

NFKBIA Antibodies

NFKBIA Antibodies for Homo sapiens (Human)

NFKBIA Proteins

NFKBIA Proteins for Homo sapiens (Human)

NFKBIA Proteins for Rattus norvegicus (Rat)

NFKBIA Proteins for Gallus gallus (Chicken)

NFKBIA Background

NF-kappa-B inhibitor alpha is a protein in humans that is encoded by the NFKBIA gene. NFKBIA possesses three regions: an N-terminal region containing phosphorylation sites that regulates signal-dependent degradation, an ankyrin repeat domain, and a C-terminal PEST region regulating basal degradation [1-3]. In unstimulated cells, inactive NF-κB complexes are present in the cytoplasm and bind to a class of inhibitor proteins known as NF-κB inhibitors (NFKBI), which include NFKBIA, NFKBIB, IκBγ, IκBɛ, Bcl-3, p100 and p105 [4]. In other words, NFKBIA inhibits NF-κB by masking the nuclear localization signals (NLS) of NF-κB proteins and keeping them sequestered in an inactive state in the cytoplasm. On cellular stimulation by immune and proinflammatory responses, NFKBIA becomes phosphorylated, promoting ubiquitination and degradation of NFKBIA, eventually enabling the dimeric RELA to translocate to the nucleus and activate transcription [5-7]. The abnormal constitutive activation of NF-κB has been observed in glioblastomas [8-10]. Besides, current data provide evidence for a tumor suppressor role of NFKBIA in glioblastomas [11].

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[3] Jacobs MD and Harrison SC. Structure of an IkappaBalpha/NF-kappaB complex [J]. Cell. 1998, 95:749–758.
[4] Chiao PJ, Miyamoto S, et al. Autoregulation of I kappa B alpha activity [J]. Proc Natl Acad Sci USA. 1994, 91:28–32.
[5] Baeuerle PA and Baltimore D: NF-kappa B: ten years after [J]. Cell. 1996, 87:13–20.
[6] Matthews JR, Nicholson J, et al. Conformational changes induced by DNA binding of NF-kappa B [J]. Nucleic Acids Res. 1995, 23:3393–3402.
[7] Roulston A, Lin R, et al. Regulation of human immunodeficiency virus type 1 and cytokine gene expression in myeloid cells by NF-kappa B/Rel transcription factors [J]. Microbiol Rev. 1995, 59:481–505.
[8] Raychaudhuri B, Han Y, et al. Aberrant constitutive activation of nuclear factor kappaB in glioblastoma multiforme drives invasive phenotype [J]. J Neurooncol. 2007, 85:39–47.
[9] Nagai S, Washiyama K, et al. Aberrant nuclear factor-kappaB activity and its participation in the growth of human malignant astrocytoma [J]. J Neurosurg. 2002, 96:909–917.
[10] Bredel M, Bredel C, et al. Tumor necrosis factor-alpha-induced protein 3 as a putative regulator of nuclear factor-kappaB-mediated resistance to O6-alkylating agents in human glioblastomas [J]. J Clin Oncol. 2006, 24:274–287.
[11] Bredel M, Scholtens DM, et al. NFKBIA deletion in glioblastomas [J]. N Engl J Med. 2011, 364:627–637.


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