Anti-DR4 antibody [EPR23650-43] - BSA and Azide free (Capture)

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

DR4 also known as TRAIL-R1 is a receptor with a molecular weight of approximately 60 kDa. It is part of the tumor necrosis factor receptor (TNFR) superfamily. DR4 is widely expressed in various types of tissues such as the liver spleen thymus and peripheral blood leukocytes. It functions mechanically by binding to its ligand TNF-related apoptosis-inducing ligand (TRAIL) which initiates signaling cascades that lead to apoptosis or programmed cell death.

Biological function summary

The death receptor 4 plays an important role in mediating cell apoptosis. Upon ligand binding DR4 interacts with the adapter molecule FADD (FAS-associated protein with death domain) facilitating the formation of the death-inducing signaling complex (DISC). This complex recruits and activates caspase-8 which eventually leads to the activation of the downstream effector caspases driving the cell towards apoptosis. DR4 operates as a significant component of the extrinsic pathway of apoptosis a process important for maintaining cellular homeostasis and eliminating harmful cells.

Pathways

DR4 functions critically within the extrinsic apoptotic pathway. This pathway involves other death receptors such as DR5 which also binds TRAIL similarly leading to apoptosis through DISC formation and caspase activation. The extrinsic pathway interconnects with the intrinsic pathway via the mitochondria with proteins like Bid acting as a bridge between them. The engagement of these pathways highlights DR4’s importance in regulatory mechanisms of cell death tightly controlling cellular proliferation and survival.

Associated diseases and disorders

DR4 plays a significant role in cancer and autoimmune diseases. Alterations in DR4 expression or function can lead to evasion of apoptosis by cancer cells contributing to tumor progression. The defective apoptotic signaling via DR4 is also linked to autoimmune disorders where insufficient apoptosis may allow for the survival of autoreactive immune cells. In both scenarios DR4's involvement usually associates with its counterpart DR5 as they share similar ligand-binding properties and signal transduction mechanisms in diseased states.