Anti-RAIDD antibody [EPR1640Y] - BSA and Azide free

Supplementary info

Activity summary

RAIDD also known as RIP-associated ICH-1/CED-3-homologous protein with a death domain (RIPDD) is an adaptor protein with a molecular mass of approximately 22 kDa. It is important for the formation of multiprotein signaling complexes. RAIDD contains a caspase recruitment domain and a death domain which facilitate its function in apoptotic pathways. It expresses in various tissues with a significant presence in immune and neural tissues where it has roles in regulating cell death and inflammation responses.

Biological function summary

RAIDD interacts closely with other proteins to regulate apoptosis. It forms part of the death-inducing signaling complex (DISC) a structure that recruits and activates initiator caspases like caspase-2. By acting as a bridge between receptor-interacting protein (RIP) and caspases RAIDD transmits signals that lead to programmed cell death. This regulation is central to cellular homeostasis and responses to damaging stimuli.

Pathways

RAIDD stands as a significant player in the apoptotic and inflammatory pathways. Apoptosis is well-documented where RAIDD serves as a connecting link to caspase-2 activation through the DISC. The second pathway of relevance is the TNF-receptor signaling pathway where RAIDD associates with RIP to influence downstream signaling events affecting expression of genes involved in immune response and cell cycle control.

Associated diseases and disorders

RAIDD's role in apoptosis and inflammation connects it to cancer and neurodegenerative diseases. In cancer RAIDD is involved in pathways that regulate tumor cell survival and death. Its interaction with proteins like caspase-2 can impact the fate of cancer cells potentially leading to abnormal cell proliferation or apoptosis resistance. In neurodegenerative conditions like Alzheimer's disease RAIDD's association with pro-inflammatory pathways and cell death mechanisms implicates it in neural cell injury and disease progression often in conjunction with RIP and caspases.