|Reactivity||Human, Mouse, Rat|
|Calculated MW||22745 Da|
|Application & Usage||Western blot analysis (0.5-4 µg/ml). However, the optimal conditions should be determined individually. The antibody detects a 22 kDa band, corresponding to the expected molecular mass of RAIDD on immunoblots.|
|Other Names||CRADD, MGC9163,|
|Formulation||100 µg (0.2 mg/ml) affinity purified rabbit anti-RAIDD polyclonal antibody in phosphate buffered saline (PBS), pH 7.2, containing 30% glycerol, 0.5% BSA, 0.01% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||RAIDD Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Apoptotic adaptor molecule specific for caspase-2 and FASL/TNF receptor-interacting protein RIP. In the presence of RIP and TRADD, CRADD recruits caspase-2 to the TNFR-1 signalling complex.|
|Cellular Location||Cytoplasm. Nucleus|
|Tissue Location||Constitutively expressed in most tissues, with particularly high expression in adult heart, testis, liver, skeletal muscle, fetal liver and kidney|
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Provided below are standard protocols that you may find useful for product applications.
Caspase family of cysteine proteases plays a key role in apoptosis. Caspase-9 is one of the most important caspases among the caspase family members. Upon induction of apoptosis, cytochrome c released from mitochondria associates with procaspase-9/Apaf-1. The complex processes procaspase-9 into a large subunit (35 kDa or 17-25 kDa) and small (10 kDa) by self-cleavage at D315. Activated caspase-9 further cleaves other caspase members including caspase-3, one of the proteases responsible for the proteolytic cleavage of many key proteins in apoptosis. In addition to self-cleavage, procaspase-9 can also be cleaved in vivo by caspase-3 at D330. The process served as a positive feedback to amplify the apoptotic signal in caspase activation pathway.
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