Phospho-I-kappa-B-alpha (Ser32) (14D4) Rabbit mAb

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). 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.