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Description
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
Specifications
Specifications
| Antigen | RIP2/RICK |
| Applications | Western Blot |
| Classification | Monoclonal |
| Clone | 25 |
| Concentration | 250μg/mL |
| Conjugate | Unconjugated |
| Formulation | Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide. |
| Host Species | Mouse |
| Immunogen | Human RIP2/RICK aa. 333-532 |
| Purification Method | Affinity Purified |
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Safety and Handling
For Research Use Only.
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