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Description
TNFα (Tumor Necrosis Factor) stimulates programmed cell death and NF-κB activation as a result of its binding to the TNF receptor 1 (TNFR1). Within this receptor, a sequence referred to as the “death domain” has been shown to be necessary for both of these functions. Using the yeast two-hybrid system to detect proteins which interact with the receptor through this “death domain”, a 34kDa protein was found and designated TRADD (TNFR1-Associated Death Domain protein). TRADD appears to contain no intrinsic catalytic activity. It also contains a death domain and it has been shown to bind to FADD and RIP. Mutational analysis of TRADD demonstrates that programmed cell death and NF-κB activation are distinct and controlled independently.
Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
Specifications
Specifications
| Antigen | TRADD |
| Applications | Western Blot |
| Classification | Monoclonal |
| Clone | 37 |
| Concentration | 250μg/mL |
| Conjugate | Unconjugated |
| Description | TNFR1-Associated Death Domain protein |
| Formulation | Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide. |
| Host Species | Mouse |
| Immunogen | Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide. |
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For Research Use Only.
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