Cell Signaling Technology

Product Pathways - NF-kappaB Signaling

RelB (C1E4) Rabbit mAb #4922

Applications Reactivity MW (kDa) Source Isotype
W IP H M R Mk 70 Rabbit IgG

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

RelB (C1E4) Rabbit mAb detects endogenous levels of RelB protein.

Source / Purification

Monoclonal antibody is produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues surrounding Ser424 of human RelB.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using RelB (C1E4) Rabbit mAb.

Background

Transcription factors of the nuclear factor kappaB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50) and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through an ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKK-α (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which is then translocated to the nucleus (9-11).

RelB, which is generally activated by non-canonical signaling, forms heterodimers with either p50 or p52 NF-κB subunits to regulate transcription (12,13). RelB knock out mice have signifcant impairments toward inflammatory responses and hematopoietic differentiation (14,15).

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  2. Baeuerle, P.A. and Baltimore, D. (1996) Cell 87, 13-20.
  3. Haskill, S. et al. (1991) Cell 65, 1281-9.
  4. Thompson, J.E. et al. (1995) Cell 80, 573-82.
  5. Whiteside, S.T. et al. (1997) EMBO J 16, 1413-26.
  6. Traenckner, E.B. et al. (1995) EMBO J 14, 2876-83.
  7. Scherer, D.C. et al. (1995) Proc Natl Acad Sci USA 92, 11259-63.
  8. Chen, Z.J. et al. (1996) Cell 84, 853-62.
  9. Senftleben, U. et al. (2001) Science 293, 1495-9.
  10. Coope, H.J. et al. (2002) EMBO J 21, 5375-85.
  11. Xiao, G. et al. (2001) Mol Cell 7, 401-9.
  12. Ryseck, R.P. et al. (1992) Mol Cell Biol 12, 674-84.
  13. Bours, V. et al. (1994) Oncogene 9, 1699-1702.
  14. Weih, F. et al. (1995) Cell 80, 331-340.
  15. Burkly, L. et al. (1995) Nature 373, 531-536.

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