Rip2/Rick Mouse, Unlabeled, Clone: 25, Bd, Mouse Monoclonal Antibody, Each

Details:

Members of the tnfr family (tnfrs, drs, fas, lymphotoxin-β-receptor, cd40, cd30, and ox-40) regulate a variety of cellular responses, such as cell activation, proliferation, differentiation, nf-κb activation, and apoptosis. Signaling through tnfr family members involves several families of receptor-associated proteins. Rip and rip2 (rick/cardiak) are ser/thr kinase adaptor molecules that associate with tnfr complexes. Both rips contain homologous n-teriminal ser/thr kinase domains, but rip contains a c-terminal death domain, while rip2 contains a c-terminal caspase activation and recruitment domain (card) similar to those found in iaps. Both rip and rip2 can activate nf-κb and cause cell death. Rip2 is recruited to tnfrs through interactions with traf1, traf5, and traf6, and rip2 activation of nf-κb requires ikkα, ikkβ, and ikkγ. In addition, rip2 can be activated through interactions with ras-activated raf1, and rip2 can activate erk1 and erk2. Thus, rip proteins may regulate tnfr signaling through both ser/thr kinase activity and interaction with the apoptotic machinery.Immunofluorescence, western blotting