TRAIL and its receptors have been used as the targets of several anti-cancer therapeutics since the mid-1990s, such as Mapatumumab. The N-terminal cytoplasmic domain is not conserved across family members, however, the C-terminal extracellular domain is conserved and can be proteolytically cleaved from the cell surface. In cells expressing DcR2, TRAIL binding therefore activates NFkappaB, leading to transcription of genes known to antagonize the death signaling pathway and/or to promote inflammation. TRAIL/APO 2 Ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (Met+Arg115-Gly281) and having a molecular mass of ~21kDa. [8] TRAIL has also been implicated as a pathogenic or protective factor in various pulmonary diseases, particularly pulmonary arterial hypertension. The structure reveals a homotrimeric protein that resembles TNF with receptor-binding epitopes at the interface between monomers.
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(1996) J. Biol. In the new TNF superfamily nomenclature, TRAIL is referred to as TNFSF10.
TRAIL forms a homotrimer that binds three receptor molecules. DcR1 functions as a TRAIL-neutralizing decoy-receptor. These artificial TRAIL mimics bind to DR4/DR5 on cancer cells and induce cell death via both apoptosis and necrosis, which makes them a potential candidate for anticancer drug development. Don’t worry, It happens to the best of us.
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It causes apoptosis primarily in tumor cells,[7] by binding to certain death receptors.
TRAIL shows homology to other members of the tumor necrosis factor superfamily. Here we describe the structure of Apo2L at 1.3 A resolution and use alanine-scanning mutagenesis to map the receptor contact regions. [9], TRAIL has also been designated CD253 (cluster of differentiation 253) and TNFSF10 (tumor necrosis factor (ligand) superfamily, member 10).[7].
Sterile Filtered White lyophilized (freeze-dried) powder. and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198. Feb 2016, "Differential cleavage of Mst1 by caspase-7/-3 is responsible for TRAIL-induced activation of the MAPK superfamily", "Luminescent Iridium Complex-Peptide Hybrids (IPHs) for Therapeutics of Cancer: Design and Synthesis of IPHs for Detection of Cancer Cells and Induction of Their Necrosis-Type Cell Death", "On the TRAIL to successful cancer therapy?