Description: The polyclonal antibody reacts with mouse, rat, and human NFkB p65; the antibody was raised against a peptide mapping to the carboxy terminus of human NFkB p65. Members of the rel/NFkB family of transcription factors are involved in the regulation of cellular responses, such as growth, development, and the inflammatory response. They share a structural motif known as the rel homology region (RHR), the C-terminal one third of which mediates protein dimerization (2, 6, 8). Complexes of p50 (NF-kB1) or p52 (NF-kB2) are generated through the processing of p105 and p100 precursors, respectively. These are usually associated with members of the Rel family (p65, c-Rel, Rel B). The homo- and heterodimer formed through combinations of NFkB/Rel proteins bind distinct kB sites to regulate the transcription of different genes (7, 9). In resting cells, NFkB is retained in the cytoplasm bound to inhibitory proteins of the IkB family. Degradation of IkB proteins occurs with cell activation, via of variety of signals, including inflammatory cytokines and bacterial lipopolysaccharides (LPS) as well as oxidative and fluid mechanical stress. This results in nuclear translocation of NFkB and the transcriptional gene activation of proinflammatory genes (1, 9). It has been suggested that NFkB plays a role in the development of numerous pathological states. Activation of NFkB induces gene programs leading to transcription of factors that promote inflammation, such as leukocyte adhesion molecules, cytokines, and chemokines. It is also thought that there are some substances with possible anti-inflammatory effects that are also NFkB regulated. There is some evidence indicating NFkB as a key factor in the pathophysiology of cardiac ischemia-reperfusion injury as well as the development of insulin dependent Diabetes Mellitus (4, 3).
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