Bioactivity: Measured in a cytotoxicity assay using L‑929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. The ED50 for this effect is 12.76 ng/mL.
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Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description: TRAIL (TNF-related apoptosis-inducing ligand), also known as APO-2 ligand and TNFSF10, is a type II transmembrane protein with a carboxy-terminal extracellular domain which exhibits homology to other TNF family members. In the TNF superfamily nomenclature, TRAIL is referred to as TNFSF10. Human TRAIL cDNA encodes a 281 amino acid (aa) residue protein with an amino-terminal intracellular domain of 17 residues and a predicted internal hydrophobic domain between residues 18 and 38. The extracellular carboxy-terminal domain contains a potential N-linked glycosylation site at amino acid residue 109. Among TNF family members, TRAIL is the most homologous to Fas ligand, sharing 28% aa sequence identity in their extracellular domains. Mouse TRAIL has also been cloned. The human TRAIL shares 65% aa sequence identity with mouse TRAIL and is active on mouse cells. Both membrane bound and soluble TRAIL have been shown to induce rapid apoptosis of many transformed cell lines. Like most TNF family members, the bioactive TRAIL exists as a homotrimer. TRAIL transcripts have been shown to be constitutively expressed in a variety of human tissues. A family of TRAIL receptors, including two receptors that transduce the apoptotic signals and two TRAIL decoy receptors that function to antagonize TRAIL-induced apoptosis, have been identified. Osteoprotegerin has been identified as a fifth TRAIL receptor. It was shown that homotrimeric TRAIL binds a zinc ion which is critical for the correct structure of the protein.
Specifications & Purity
ActiBioPure™, Bioactive, Carrier Free, Azide Free, High performance, ≥90%(SDS-PAGE)
Bioactivity
Measured in a cytotoxicity assay using L‑929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. The ED50 for this effect is 12.76 ng/mL.
18.7 kDa and 40.0 kDa, reducing conditions; 18.7 kDa, 40.0 kDa and 59.3 kDa, non-reducing conditions
Images
Recombinant Human TRAIL/TNFSF10 Protein (rp169692) - Protein Bioactivity Measured in a cytotoxicity assay using L‑929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D (A113142). The ED50 for this effect is typically less than 20.0 ng/mL.
Recombinant Human TRAIL/TNFSF10 Protein (rp169692) - SDS-PAGE Recombinant Human TRAIL/TNFSF10 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing two bands at 18.7 and 40.0 kDa under reducing conditions, three bands at 18.7, 40.0 and 59.3 kDa under non-reducing conditions.
Product Specifications
Form
Transparent gelatinous
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute at 1.0 mg/mL in sterile distilled water. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilu
Storage Temp
Store at -20°C,Avoid repeated freezing and thawing
Shipped In
Ice chest + Ice pads
Stability And Storage
Store at -20°C stable up to 1 year. Avoid freeze/thaw cycle.
Certificates
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1.Pitti, R M RM and 5 more authors.. (1996) Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family.. The Journal of biological chemistry, (31):[PMID:8663110]
2.Wiley, S R SR and 9 more authors.. (1995) Identification and characterization of a new member of the TNF family that induces apoptosis.. Immunity, [PMID:8777713]
3.Cha, S S SS and 7 more authors.. (1999) 2.8 A resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity.. Immunity, [PMID:10485660]
4.Mongkolsapaya, J J and 6 more authors.. (1999) Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation.. Nature structural biology, [PMID:10542098]
5.Hymowitz, S G SG and 7 more authors.. (1999) Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5.. Molecular cell, [PMID:10549288]
6.Muzny, Donna M DM and 113 more authors.. (2006) The DNA sequence, annotation and analysis of human chromosome 3.. Nature, (27):[PMID:16641997]
7.Schnepple, David J DJ and 11 more authors.. (2011) Isolation of a TRAIL antagonist from the serum of HIV-infected patients.. The Journal of biological chemistry, (14):[PMID:21859711]
8.Bordoli, Mattia R MR and 14 more authors.. (2014) A secreted tyrosine kinase acts in the extracellular environment.. Cell, (28):[PMID:25171405]
9.Ramamurthy, Vidhyashankar V and 9 more authors.. (2015) The structure of the death receptor 4-TNF-related apoptosis-inducing ligand (DR4-TRAIL) complex.. Acta crystallographica. Section F, Structural biology communications, [PMID:26457518]
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