CRADD Antibody

Caspases are a family of cysteine proteases that play essential roles in apoptosis (programmed cell death) and inflammation. They are involved in the execution phase of cell apoptosis, where they cleave specific substrates leading to cellular disassembly. Receptor-interacting protein (RIP) kinases are a group of serine/threonine-protein kinases that are crucial in regulating cell death and inflammation. The RIP adapter with a death domain is a key component in the signaling pathways that mediate apoptosis and necroptosis.

Caspases are synthesized as inactive proenzymes that undergo proteolytic processing to produce active enzymes. They are classified into initiator caspases (such as caspase-8 and caspase-9) and effector caspases (such as caspase-3, caspase-6, and caspase-7). Initiator caspases are activated by apoptotic signals and, in turn, activate effector caspases, which then execute apoptosis by cleaving cellular components .

The RIP adapter with a death domain is a critical mediator in the tumor necrosis factor (TNF) signaling pathway. It is involved in the activation of nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) and the induction of apoptosis. The death domain is a protein interaction module found in many proteins involved in apoptosis and inflammation. It allows the formation of signaling complexes that transduce apoptotic signals .

The interaction between caspases and the RIP adapter with a death domain is pivotal in regulating cell death. Caspase-8, an initiator caspase, cleaves RIP kinases, which can lead to the inhibition of NF-κB activation and the promotion of apoptosis. This cleavage is essential for the proper execution of apoptosis and the prevention of necroptosis, a form of programmed necrosis .