TNFRSF10B Human

TNFRSF10B contains an intracellular death domain, which is essential for transmitting apoptotic signals . The receptor is activated by binding to its ligand, tumor necrosis factor-related apoptosis-inducing ligand (TNFSF10/TRAIL/APO-2L) . Upon activation, TNFRSF10B recruits the adaptor molecule FADD (Fas-Associated protein with Death Domain), which in turn recruits and activates caspase-8 . This leads to the formation of the death-inducing signaling complex (DISC), initiating a cascade of caspase activations that ultimately result in apoptosis .

The ability of TNFRSF10B to induce apoptosis makes it a critical player in maintaining cellular homeostasis and preventing tumor development . Dysregulation of TNFRSF10B signaling has been implicated in various cancers, including squamous cell carcinoma of the head and neck and laryngeal squamous cell carcinoma . Additionally, TNFRSF10B is involved in the regulation of immune responses and inflammation .

Given its role in apoptosis, TNFRSF10B is a potential target for cancer therapy . Strategies to enhance TNFRSF10B signaling could promote the selective killing of cancer cells while sparing normal cells . Research has shown that endoplasmic reticulum stress can regulate the expression and localization of TNFRSF10B, influencing its ability to induce apoptosis and affect chemotherapy resistance in cancers such as triple-negative breast cancer (TNBC) .

Human recombinant TNFRSF10B is produced using recombinant DNA technology, allowing for the study of its structure, function, and therapeutic potential in a controlled laboratory setting . This recombinant protein is used in various research applications, including the investigation of apoptotic pathways, cancer biology, and drug development .