Anti-NFkB: Polyclonal Nuclear Factor-kappa B, p65, Antibody

In addition to regulation of NF-kappa-B activity through removal of IkappaB from NF-kappa-B/I B complexes, NF-kappa-B activity is also regulated through modulation of its transcriptional function. Changes in NF-kappa-B transcriptional activity have been assigned to inducible phosphorylation of the p65 subunit at Ser276, Ser529, and Ser536 by a large variety of kinases in response to different stimuli.⁴ Additionally, NF-kappa-B -dependent transcription requires multiple coactivators possessing histone acetyltransferase activity: CREB binding protein (CBP) and its homolog p300, p300/CBP-associated factor (P/CAF), SRC-1/NcoA-1, and TIF-2/GRIP-1/NcoA-2. Importantly, recruitment of CBP is enhanced by phosphorylation by the catalytic subunit of PKA (PKAc) of p65 at Ser276. More recently, other findings demonstrated a role for histone deacetylases (HDACs) as well. The first evidence came from the demonstration that inhibition of HDAC activity by trichostatin A (TSA) increases NF-kappa-B-dependent gene expression. It was next shown that NF-kappa-B interacts with distinct HDAC isoforms to negatively regulate gene expression, presumably through the deacetylation of histones and/or nonhistone proteins. Importantly, the phosphorylation status of p65 determines whether it associates with CBP/p300 or HDAC-1, ensuring that only signal-induced NF-kappa-B entering the nucleus can activate transcription.⁵