Recombinant Human TNFRSF10A (TRAIL R1)-Fc Chimera (carrier-free)
Description
TNFRSF10A, also called TRAIL R1 and DR4, is a member of the TNF receptor superfamily. It contains a cysteine-rich extracellular domain, a transmembrane domain and an intracellular death domain, which mediates interactions between death receptor and death domain-containing adaptor proteins. When the trimeric ligand TRAIL (TNFSF10) is bound, homotrimer TNFRSF10A interacts with the adaptor protein Fas-associated death domain (FADD), in turn recruits caspase-8 and assembles a death-inducing signaling complex (DISC) that initiates apoptosis. There are decoy receptors, TRAIL R3 (DcR1), TRAIL R4 (DcR2) and OPG, which antagonize the apoptotic effect via competitive ligand binding. Human TNFRSF10A shows 52% identity to human TNFRSF10B and there is some functional redundancy. Several evidences indicated that TNFRSF10A play roles in tumorigenesis and DNA damage response. Some studies indicated the role of TNFRSF10A in cancer predisposition. A rare allele of TNFRSF10A was found to be more frequent in chronic lymphocytic leukemia (CLL), mantle cell lymphoma (MCL), prostate cancer, bladder cancer, colorectal cancer and head and neck squamous cell carcinoma (HNSCC). Agonistic monoclonal antibodies against TNFRSF10A, which can induce apoptosis in the absence of TRAIL, are used for cancer therapies. However, some studies have suggested that TNFRSF10B contributes more than TNFRSF10A to TRAIL-induced apoptosis in cancer cells that express both receptors. The expression of TNFRSF10A is inducible and up-regulated by DNA damage in p53-dependent manner.