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RAIDD (human) monoclonal antibody (Raiddy-1)

ALX-804-827-C100 100 µg 357.00 USD
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Product Specification

Alternative Name:CRADD, Caspase and RIP adaptor with death domain, RIP-associated protein with a death domain
Immunogen:Recombinant human full length soluble RAIDD (aa 1-199).
UniProt ID:P78560
Source:Purified from concentrated hybridoma tissue culture supernatant.
Species reactivity:Human
Applications:IP, WB
Recommended Dilutions/Conditions:Immunoprecipitation (1:100)
Western Blot (1:1,000)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
Formulation:Liquid. Purified antibody in PBS containing 0.02% sodium azide.
Use/Stability:Stable for at least 1 year after receipt when stored at -20°C.
Handling:Avoid freeze/thaw cycles.
Shipping:Shipped on Blue Ice
Short Term Storage:+4°C
Long Term Storage:-20°C
Scientific Background:RAIDD (RIP-associated ICH-1 homologous protein with a death domain) is an adaptor molecule that mediates the action of cysteine proteases involved in apoptosis. In human cell lines, the caspase-2 adaptor RAIDD interacts selectively with caspase-2 through its caspase recruitment domain (CARD) and leads to caspase-2-dependent death. RAIDD overexpression induced caspase-2, CARD- and caspase-9-dependent apoptosis of PC12 cells and sympathetic neurons. Apoptosis correlated with the formation of discrete perinuclear aggregates. Both death and aggregates required the expression of full-length RAIDD. It has been reported that activation of caspase-2 occurs in a complex that contains the death domain–containing protein PIDD, whose expression is induced by p53, and the adaptor protein RAIDD.

General Literature References

RAIDD aggregation facilitates apoptotic death of PC12 cells and sympathetic neurons: O. Jabado, et al.; Cell Death Differ. 11, 618 (2004), Abstract;
The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress: A. Tinel and J. Tschopp; Science 304, 843 (2004), Abstract;

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