RELB is a key member of the NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) transcription factor family, which regulates genes involved in immune responses, inflammation, cell survival, and proliferation. Unlike other NF-κB proteins like RELA or p50. RELB primarily functions within the non-canonical NF-κB signaling pathway. It forms heterodimers with p52 (processed from NF-κB2/p100) to activate target genes, a process triggered by specific stimuli such as lymphotoxin-β, CD40 ligand, or BAFF. This pathway is critical for lymphoid organ development, B-cell maturation, and dendritic cell activation.
RELB antibodies are immunological tools designed to detect and study RELB protein expression, localization, and function in experimental settings. They are widely used in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to investigate RELB's role in physiological and pathological contexts. Dysregulation of RELB has been implicated in autoimmune diseases, chronic inflammation, and cancers, particularly lymphomas and leukemias. For example, aberrant RELB activation may promote tumor cell survival or resistance to therapy. Researchers also utilize RELB antibodies to explore its interaction with other signaling molecules or epigenetic regulators. Commercial RELB antibodies are typically validated for specificity across human, mouse, and rat samples, with monoclonal and polyclonal variants available. Proper validation using knockout controls or siRNA knockdown remains essential due to potential cross-reactivity with structurally related NF-κB proteins.