TRAIL, Soluble human

TNF-related apoptosis-inducing ligand (TRAIL; Apo2L; CD253; TNFSF10) is a type II transmembrane protein of about 34kDa. Like most members of the tumor necrosis factor (TNF) superfamily of cytokines, TRAIL can be cleaved at the cell surface by metalloproteases to form a soluble molecule. The gene encoding TRAIL is localized on human chromosome 3q26.31.

TRAIL, soluble human has been used in cell culture, chemical transfection and in caspase-3/7 activity assay.

Trimerized TNF-related apoptosis-inducing ligand (TRAIL) triggers apoptosis upon ligation of cell surface TRAIL-receptor 1 (R1) and/or TRAIL-R2 by inducing the formation of the so-called multiprotein death-inducing signaling complex (DISC). Active TRAIL forms trimers and specifically binds to five distinct receptors: TRAIL-receptors 1,-2,-3,-4 {TRAIL-R1 (DR4; Apo2; CD261; TNFRSF10A), TRAIL-R2 (DR5; KILLER; TRICK2A; TRICK2B; CD262; TNFRSF10B), TRAIL-R3 (DcR1; LIT; TRID; CD263; TNFRSF10C), TRAIL-R4 (DcR2; TRUNDD; CD264; TNFRSF10D)} and osteoprotegerin (OPG; OCIF; TNFRSF11B).

Solution in 20 mM HEPES, pH 7.9, 120 mM NaCl, 0.01% Tween 20, 1% sucrose, 1 mM DTT.

The extracellular domain of human TRAIL (aa 95-281) is fused at the N-terminus to a His-tag and a linker peptide. The active multimeric conformation is stabilized by an inserted mutation allowing an additional CC-bridge.