Tumor necrosis factor-related apoptosis inducing ligand (TRAIL) is a type II membrane protein, whose C-terminal extracellular domain shows clear homology to other TNF superfamily members. TRAIL transcripts are detected in a variety of human tissues, most predominantly in spleen, lung, and prostate.
Interacting protein(s): DR4 (P7049F), DR5 (P7053F), TRAIL R3 (P7057F), TRAIL R4 (P7059F)
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|MW (calculated):||46,157 daltons|
|MW (SDS-PAGE):||50 Kd|
|Abs 0.1% (= 1 mg/ml):||1.307|
|Purity:||>95 % by SDS-PAGE|
Tumor necrosis factor-related apoptosis inducing ligand (TRAIL) is a type II membrane protein, whose C-terminal extracellular domain shows clear homology to other TNF superfamily members. TRAIL transcripts are detected in a variety of human tissues, most predominantly in spleen, lung, and prostate. TRAIL, also known as Apo2L, triggers apoptotic cascade via interacting with its death receptors including DR4 and DR5.
Agonistic monoclonal antibodies can selectively activate TRAIL death receptors and trigger apoptosis. TRAIL clearly distinguishes itself from the other family members including TNF-α and FasL both of which could not make it to the clinic due to their toxic nature. It is therefore, evident that the future of TRAIL-based therapeutic approaches looks brighter.
The TRAIL gene is located on chromosome 3 at position 3q26, which is not close to any other known TNF superfamily members. Both full-length cell surface expressed TRAIL and picomolar concentrations of soluble TRAIL rapidly induce apoptosis in a wide variety of transformed cell lines of diverse origin.
Amino Acid Sequence
1. Identification and characterization of a new member of the TNF family that induces apoptosis. Wiley S.R., Schooley K., Smolak P.J., Din W.S., Huang C.-P., Nicholl J.K., Sutherland G.R., Davis-Smith T., Rauch C., Smith C.A., Goodwin R.G. Immunity 3:673-682 (1995)
2. Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family. Pitti R.M., Marsters S.A., Ruppert S., Donahue C.J., Moore A., Ashkenazi A. J. Biol. Chem. 271:12687-12690 (1996)
3. Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation. Mongkolsapaya J., Grimes J.M., Chen N., Xu X.-N., Stuart D.I., Jones E.Y., Screaton G.R. Nat. Struct. Biol. 6:1048-1053 (1999)
4. 2.8 A resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity. Cha S.-S., Kim M.S., Choi Y.H., Sung B.J., Shin N.K., Shin H.C., Sung Y.C., Oh B.-H. Immunity 11:253-261 (1999)