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RIP (receptor interacting protein) is a 74 kDa serine/threonine kinase which may be recruited to TNFR type 1 and Fas (CD95) receptor signal complexes following ligand binding. RIP interacts with other signal proteins within these complexes (e.g., RAIDD) and has also been shown to interact with pro-caspase-2. RIP contains an N-terminal kinase domain as well as a C-terminal death domain that is homologous to intracellular death domain of Fas. Over expression of RIP in vitro is sufficient to induce cell death, demonstrating that RIP functions as an apoptosis-inducing protein. Interaction of the Fas death domain with other intracellular proteins like RIP is an important step leading to downstream components in apoptotic signaling pathways. Clone G322-2 recognizes human RIP. A recombinant truncated human RIP:tagged fusion protein, lacking the kinase domain of RIP, was used as immunogen. The specificity of the antibody was verified by ELISA, immunoprecipitation and western blot analysis. The antibody is routinely tested by western blot analysis in human Jurkat T cells where it recognizes RIP as a 74 kDa band. Smaller molecular weight breakdown bands of ∽30 kDa, 22 kDa, and/or 16 kDa are sometimes observed.
