RelA/NFkB p65 Protein, Human (GST)

RelA/NF-kappaB p65 is a multifaceted transcription factor integral to diverse cellular processes, acting as the endpoint of signal transduction cascades governing inflammation, immunity, differentiation, growth, tumorigenesis, and apoptosis. Functioning within NF-kappaB heterodimeric complexes, RelA pairs predominantly with NFKB1/p50 and REL, exerting transcriptional activation of target genes. This complex is held inactive in the cytoplasm by binding with NF-kappaB inhibitor (I-kappa-B) proteins. Upon stimulation, I-kappa-B is phosphorylated by I-kappa-B kinases, triggering its degradation, liberating the active NF-kappaB complex. RelA demonstrates a weak DNA-binding site, directly participating in DNA binding within the NF-kappaB complex. Beyond direct transcriptional activation, RelA modulates promoter accessibility, indirectly influencing gene expression. Intriguingly, RelA also interacts with a myriad of proteins, including various inhibitors, kinases, deacetylases, and other cofactors, underscoring its role in intricate cellular networks. Furthermore, in the context of microbial infection, RelA plays a key role in regulating the IFN response during SARS-CoV-2 infection and has been implicated in latent HIV-1 transcriptional reactivation.