NFκB-p65, also known as RelA, is a subunit of the NFκB transcription factor complex, an important mediator of inflammatory and immune responses. NFκB-p65 is normally sequestered in the cytoplasm through an interaction with IκB. NFκB translocates to the nucleus when IκB is degraded in response to stimuli such as TNFa. In mammals, there are five members of the NFκB family that can form heterodimers in the nucleus to activate different sets of genes. The Ser529 site on the C-terminal transactivation domain of NFκB-p65 is often phosphorylated in response to the same stimuli that result in degradation of IκB. This phosphorylation improves the transcriptional activity of p65 but does not affect nuclear translocation or DNA binding. The K10-895.12.50 monoclonal antibody recognizes the phosphorylated serine (pS529) of human NF-kB p65 subunit.
Anti-Human pNFkBp65 [S529] (K10x)-166Er—25 µg
Target:pNFkB p65 [S529]