NF-κB p65 (pS536) Mouse anti-Human, Unlabeled, Clone: J144-460, BD

Description

• 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 IkB 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, IkB 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 kB 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
• Western Blotting