RIP with control Mouse anti-Human, Unlabeled, Clone: G322-2, BD

Description

• 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.