SuperKillerTRAIL(TM), Soluble (mouse, rec.)

(3 x 20µg). The extracellular domain of mouse TRAIL (amino acids 99-291) 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. Induces apoptosis at concentrations of >10ng/ml as tested on human tumor cells. This effect can be efficiently blocked by recombinant mouse TRAIL receptors. This protein does not require a cross-linker (enhancer) for its potent biological activity. Liquid. In 20mM HEPES, pH 7.4, 300mM NaCl, 0.01% Tween 20, 1% sucrose, 1mM DTT. 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. Active TRAIL forms trimers and specifically binds to five distinct receptors: 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). Trimerized TRAIL triggers apoptosis upon ligation of cell surface TRAIL-R1 and/or TRAIL-R2 by inducing the formation of the so-called multiprotein death-inducing signaling complex (DISC).