BD Pharmingen™ Purified Mouse anti-NF-κB p65 (pS536)

Nuclear factor κB (NF-κB) is a ubiquitously expressed transcription factor that regulates the expression of 200-300 genes.  It is crucial for basic cellular responses to stress and pathogens, such as proliferation, survival, development, and apoptosis.  The most studied NF-κB complex consists of the p50 (also known as NF-κB1) and p65 (also known as REL-A) subunits, both containing a 300-amino acid region with homology to the Rel proto-oncogene product (RH domain).  The RH domain contains motifs for dimerization, nuclear localization, and binding to specific DNA sequences.  In addition to the RH domain, the p65 subunit contains the transactivation domain, which is responsible for the interaction with the inhibitor IκB and which contains phosphorylation sites.  In most cell types, the p50/p65 heterodimer is located within the cytoplasm complexed to IκB.  This complex prevents nuclear translocation and activity of NF-κB.  In response to stimuli such as cytokines, LPS, DNA damage, and viral infections, IκB is phosphorylated at critical residues.  This phosphorylation induces dissociation of the IκB/NF-κB complex, allowing the free heterodimeric NF-κB to translocate to the nucleus.  Furthermore, optimal activation of NF-κB requires phosphorylation in the transactivation domain of p65.  In the nucleus, activated NF-κB dimers bind to the κB sites within promoters and enhancers and function as transcriptional activators.  

The J144-460 monoclonal antibody recognizes the phosphorylated serine 536 (pS536) in the transactivation domain of human NF-κB p65.