Anti-p65 NF-kB

0.5mg/ml if reconstituted with 0.2ml sterile DI water. RELA, also called NFKB3 or NFKB, p65 subunit is part of the NF-kB complex. The complex is inhibited by I-kappa-B proteins, which inactivates NFkB by trapping it in the cytoplasm. The p65 heterodimer is the most abundant form of NF-kB. It is a nonhistone substrate of HDAC3 and that IKBA-dependent nuclear export of the HDAC3-deacetylated RELA replenishes the depleted cytoplasmic pool of latent NFKB-IKBA complexes for subsequent NF-kB responses. Its nucleocytoplasmic redistribution coincided with export of PPARG, and immunoprecipitation analysis indicated that PPARG-RELA association was dependent on the PPARG C-terminal ligand-binding domain. IKK-dependent phosphorylation of RELA on Ser468 enhanced binding of GCN5 to RELA and its ubiquitination. Protein function: NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain- containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric RELA-NFKB1 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. The NF-kappa-B heterodimeric RELA-NFKB1 and RELA-REL complexes, for instance, function as transcriptional activators. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I- kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The inhibitory effect of I- kappa-B on NF-kappa-B through retention in the cytoplasm is exerted primarily through the interaction with RELA. RELA shows a weak DNA- binding site which could contribute directly to DNA binding in the NF- kappa-B complex. Beside its activity as a direct transcriptional activator, it is also able to modulate promoters accessibility to transcription factors and thereby indirectly regulate gene expression. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T- cells (PubMed:15790681). The NF-kappa-B homodimeric RELA-RELA complex appears to be involved in invasin-mediated activation of IL-8 expression. Key transcription factor regulating the IFN response during SARS-CoV-2 infection (PubMed:33440148). [The UniProt Consortium]