IκB-ζ Antibody

9244:

Immunoprecipitation , Western Blotting

IκB-ζ Antibody detects endogenous levels of total human IκB-ζ protein and transfected levels of mouse IκB-ζ.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues at the amino terminus of human IκB-ζ. Antibodies were purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of extracts from THP-1 cells, differentiated with TPA #4147 (80 nM for 24 hr) and treated with 1 μg/ml LPS for the indicated times, using IκB-ζ Antibody.

Western Blotting

Western blot analysis of extracts from HeLa cells, mock transfected or transfected with mouse IκB-ζ, using IκB-ζ Antibody.

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).

IκB-ζ (MAIL, INAP) is a unique IκB family member homologous to Bcl-3 and induced by IL-1 and Toll-like receptor (TLR) ligands (9-11). Like other family members, it contains carboxyl terminal ankyrin-repeats responsible for interaction with NF-κB, particularly p50. Unlike classical IκB family members (α, β, ε) which inhibit NF-κB translocation and are rapidly degraded upon cytokine treatment, IκB-ζ is cytokine-inducible and localized to the nucleus where it regulates NF-κB DNA binding and transactivation (12-14). Induction of IκB-ζ is required for TLR/IL-1 induction of a subset of NF-κB target genes, including IL-6 (15). However, the IκB-ζ can also inhibit transactivation of other targets, such as TNF-α (14,15).

1. Baeuerle, P.A. and Baltimore, D. (1988) Science 242, 540-6.
2. Beg, A.A. and Baldwin, A.S. (1993) Genes Dev 7, 2064-70.
3. Finco, T.S. et al. (1994) Proc Natl Acad Sci USA 91, 11884-8.
4. Brown, K. et al. (1995) Science 267, 1485-8.
5. Brockman, J.A. et al. (1995) Mol Cell Biol 15, 2809-18.
6. Traenckner, E.B. et al. (1995) EMBO J 14, 2876-83.
7. Chen, Z.J. et al. (1996) Cell 84, 853-62.
8. Karin, M. and Ben-Neriah, Y. (2000) Annu Rev Immunol 18, 621-63.
9. Yamazaki, S. et al. (2001) J Biol Chem 276, 27657-62.
10. Kitamura, H. et al. (2000) FEBS Lett 485, 53-6.
11. Haruta, H. et al. (2001) J Biol Chem 276, 12485-8.
12. Matsuo, S. et al. (2007) Biochem J 405, 605-15.
13. Totzke, G. et al. (2006) J Biol Chem 281, 12645-54.
14. Motoyama, M. et al. (2005) J Biol Chem 280, 7444-51.
15. Yamamoto, M. et al. (2004) Nature 430, 218-22.
16. Ray, M. et al. (2010) J Immunol , .

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For Research Use Only. Not For Use In Diagnostic Procedures.