Anti-RAIDD Antibody

This rabbit polyclonal reagent from Antibodies.com targets RAIDD (RIP-associated ICH-1/CED-3-homologous protein with a death domain), a dual-domain adaptor that bridges death-receptor signaling to caspase-2 activation. RAIDD contains both a death domain (DD) and a caspase recruitment domain (CARD) and participates in the assembly of cytoplasmic death-signaling platforms, including the PIDDosome, that drive stress- and receptor-induced apoptosis. It is encoded by the CRADD gene and is widely studied in apoptosis, neurobiology, inflammation, and tumor cell-death research.

Supplied as 100 µl of antibody at 1 mg/ml in PBS with 0.1% sodium azide and 50% glycerol, the reagent is unconjugated for flexible pairing with user-selected secondary antibodies and detection chemistries. The polyclonal format presents multiple epitope specificities across the RAIDD sequence, which is useful when target abundance is limited or when probing denatured protein in fixed tissue sections. Recommended applications are Western blot (WB) and immunohistochemistry (IHC); the antibody has been validated for reactivity against human, mouse, and rat samples, supporting translational work across commonly used cell lines and rodent disease models.

For handling, store the vial at -20 °C in the supplied glycerol-containing buffer; the 50% glycerol acts as a cryoprotectant, so aliquoting the stock before freezing is recommended to limit freeze-thaw cycles. Allow the vial to equilibrate to refrigerator temperature before opening to reduce condensation, and mix gently without vortexing to preserve IgG integrity. Sodium azide is included as a preservative; take this into account when planning experiments with live cells or azide-sensitive conjugation chemistries.

Researchers commonly pair this antibody with lysates or fixed sections from cells under genotoxic stress, cytokine stimulation, or disease-model conditions where apoptotic pathway engagement is of interest. It can be used alongside other death-domain or CARD-family reagents to map the composition of the caspase-2 activation complex and to compare baseline versus stimulated apoptosis signaling across model systems.