c-Rel (E8Z5Y) XP^® Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of total c-Rel protein.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human c-Rel protein.

Transcription factors of the nuclear factor κB (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 the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

c-Rel contains an amino-terminal DNA-binding domain, referred to as the REL homology domain (REH), and carboxy-terminal transactivation domains. The c-Rel protein is typically inhibited in unstimulated cells by IκBα and IκBβ. c-Rel expression is highest in hematopoietic cells with extensive research studies demonstrating its role in immune cell function and pathogenesis of disease (12,13).