The c-Rel antibody is a crucial tool for studying the c-Rel protein, a member of the NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) transcription factor family. c-Rel plays a pivotal role in regulating immune and inflammatory responses, cell survival, and proliferation. Structurally, it contains a conserved N-terminal Rel homology domain (RHD) responsible for DNA binding, dimerization, and interaction with inhibitory IκB proteins. In resting cells, c-Rel is sequestered in the cytoplasm via binding to IκB. Upon activation by stimuli like cytokines, pathogens, or stress signals (e.g., via TLRs, TNFR, or IL-1R pathways), c-Rel translocates to the nucleus, where it regulates gene expression.
c-Rel is particularly significant in lymphoid cells, influencing T-cell activation, B-cell differentiation, and macrophage function. Dysregulation of c-Rel is linked to autoimmune diseases, chronic inflammation, and cancers, especially lymphoid malignancies. Researchers use c-Rel antibodies in techniques like Western blotting, immunofluorescence, ChIP-seq, and flow cytometry to detect its expression, localization, and DNA-binding activity. These antibodies are often validated in knockout models or siRNA-treated cells to ensure specificity.
Commercial c-Rel antibodies are typically raised in rabbits or mice, available as monoclonal or polyclonal formats. Proper controls, including isotype-matched antibodies and blocking peptides, are essential to confirm signal specificity. Its role in NF-κB signaling and disease mechanisms makes c-Rel a key target for therapeutic development and biomedical research.