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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.
Regulatory Status:RUO - Research Use Only

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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