RIP (D94C12) XP® Rabbit mAb

The receptor-interacting protein (RIP) family of serine-threonine kinases (RIP, RIP2, RIP3, and RIP4) are important regulators of cellular stress that trigger pro-survival and inflammatory responses through the activation of NF-κB, as well as pro-apoptotic pathways (1). In addition to the kinase domain, RIP contains a death domain responsible for interaction with the death domain receptor Fas and recruitment to TNF-R1 through interaction with TRADD (2,3). RIP-deficient cells show a failure in TNF-mediated NF-κB activation, making the cells more sensitive to apoptosis (4,5). RIP also interacts with TNF-receptor-associated factors (TRAFs) and can recruit IKKs to the TNF-R1 signaling complex via interaction with NEMO, leading to IκB phosphorylation and degradation (6,7). Overexpression of RIP induces both NF-κB activation and apoptosis (2,3). Caspase-8-dependent cleavage of the RIP death domain can trigger the apoptotic activity of RIP (8). 1.Meylan, E. and Tschopp, J. (2005) Trends Biochem Sci 30, 151-9. 2.Hsu, H. et al. (1996) Immunity 4, 387-96. 3.Stanger, B.Z. et al. (1995) Cell 81, 513-23. 4.Ting, A.T. et al. (1996) EMBO J 15, 6189-96. 5.Kelliher, M.A. et al. (1998) Immunity 8, 297-303. 6.Devin, A. et al. (2000) Immunity 12, 419-29. 7.Zhang, S.Q. et al. (2000) Immunity 12, 301-11. 8.Lin, Y. et al. (1999) Genes Dev 13, 2514-26.