SuperKillerTRAIL™, Soluble (mouse) (rec.)

TRAIL; Apo-2L; TNFSF10; CD253

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.

0.5mg/ml

32160000

<0.01EU/µg purified protein (LAL test; Lonza).

liquid

Liquid. In 20mM HEPES, pH 7.4, 300mM NaCl, 0.01% Tween 20, 1% sucrose, 1mM DTT.

Avoid freeze/thaw cycles.

Protein. The extracellular domain of mouse TRAIL (aa 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. Source: E. coli. Endotoxin content: <0.01EU/µg purified protein (LAL test; Lonza). Liquid. In 20mM HEPES, pH 7.4, 300mM NaCl, 0.01% Tween 20, 1% sucrose, 1mM DTT. Binds to mouse and less potently to human TRAIL receptors. Purity: >95% (SDS-PAGE). 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).

~24kDa

P50592

Plastic Vial

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).

>95% (SDS-PAGE)

The extracellular domain of mouse TRAIL (aa 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.

E. coli

Binds to mouse and less potently to human TRAIL receptors.

His

Non-hazardous

Other Proteins

12352202

Once thawed it is recommended to prepare appropriate aliquots and to store them at -80°C. , Stable for at least 1 year after receipt when stored at -80°C.