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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.
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Figure: Detection of endogenous RAIDD (human) in HEK293T cells by the PAb to RAIDD (AT100) (Prod. No. ALX-210-915).Method: Total cell extracts (50µg) were run on a SDS-gel, and revealed with anti-RAIDD antibody (AT100, 1:1000, affinity purified antibody, in 5% milk powder) for 1 hour at RT followed by incubation with HRP-coupled anti-rabbit secondary antibody (1:4’000). The arrow indicates endogenous human RAIDD.
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RUO – Research Use Only |
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