WB-Western Blot IP-Immunoprecipitation IHC-Immunohistochemistry IF-Immunofluorescence ICC-Immunocytochemistry FC-Flow Cytometry

NFκB p65 also known as RELA is a critical subunit of the NFκB transcription factor complex, which plays a pivotal role in regulating genes involved in immune and inflammatory responses, cell proliferation, and survival. Structurally, NFκB p65 contains a Rel homology domain (RHD) at its N-terminus responsible for DNA binding and dimerization, and a transactivation domain (TAD) at its C-terminus. The TAD, located near the C-terminus, is essential for initiating transcription by interacting with other transcriptional co-activators and the basal transcription machinery. Understanding the structure of NFκB p65 is important because alterations or post-translational modifications in these domains can significantly affect its ability to regulate gene expression, impacting processes like inflammation, immune responses, and oncogenesis. In resting cells, NFκB p65 is sequestered in the cytoplasm by inhibitor proteins called IκBs. Upon activation by various stimuli such as cytokines or stress signals, IκBs are degraded, allowing NFκB p65 to translocate to the nucleus, where NFκB p65 binds to specific DNA sequences to modulate gene expression.