Product Details
Alternative Name: | DR5, TNFRSF 10B, KILLER, CD262 |
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MW: | 58kDa (SDS-PAGE). |
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Source: | Produced in HEK 293 cells. The extracellular domain of human TRAIL-R2 (DR5) (aa 52-212) is fused to the Fc portion of human IgG1. |
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UniProt ID: | O14763 |
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Concentration: | 1mg/ml after reconstitution. |
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Formulation: | Lyophilized. Contains PBS. |
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Purity: | ≥95% (SDS-PAGE) |
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Endotoxin Content: | <0.1EU/µg purified protein (LAL test; Bio Whittaker). |
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Species reactivity: | Human, Mouse
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Specificity: | Binds human and mouse TRAIL. |
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Biological Activity: | Inhibits human soluble TRAIL-mediated apoptosis. |
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Applications: | ELISA
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Application Notes: | ELISA: binds to TRAIL at 10-100 ng/ml. |
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Reconstitution: | Reconstitute with 50µl sterile water. Further dilutions should be made with medium containing 5% fetal calf serum or a carrier protein. |
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Shipping: | Blue Ice |
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Long Term Storage: | -20°C |
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Use/Stability: | Stable for at least 6 months after receipt when stored at -20°C. |
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Handling: | Avoid freeze/thaw cycles. After reconstitution, prepare aliquots and store at -20°C. |
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Technical Info/Product Notes: | Historical data has shown inhibition of human soluble TRAIL-induced apoptosis in a concentration range of 0.5-10µg/ml. |
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Regulatory Status: | RUO - Research Use Only |
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Fig 2: ELISA Analysis: 100 ng/well of receptor or control is coated on a 96-well plate. After blocking, ligand is titrated 2-fold in series, and detected with anti-flag antibody. TRAIL (Prod # ALX-522-003) shows positive for binding to TRAIL-R2 and negative for binding to either Fc control protein (Prod # ALX-203-004) and buffer control.
Fig 1: SDS-PAGE Analysis. Lane 1: MW Marker, Lane 2: 1 µg, Lane 3: 2 µg TRAIL-R2.
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Product Literature References
Biliary tract instillation of a SMAC mimetic induces TRAIL-dependent acute sclerosing cholangitis-like injury in mice: M.E. Guicciardi, et al.; Cell Death Dis.
8, 2535 (2017),
Abstract;
Full Text
Serine 574 phosphorylation alters transcriptional programming of FOXO3 by selectively enhancing apoptotic gene expression: Z. Li, et al.; Cell Death Differ.
23, 583 (2016),
Abstract;
Synthetic ligands of death receptor 5 display a cell-selective agonistic effect at different oligomerization levels: J. Beyrath, et al.; Oncotarget
7, 64942 (2016),
Abstract;
Full Text
Death receptor 5 signaling promotes hepatocyte lipoapoptosis: S.C. Cazanave, et al.; J. Biol. Chem.
286, 39336 (2011),
Abstract;
Proteasome inhibition can induce an autophagy-dependent apical activation of caspase-8: M.A. Laussmann, et al.; Cell Death Differ.
18, 1584 (2011),
Abstract;
Two adjacent trimeric fas ligands are required for fas signaling and formation of a death-inducing signaling complex: N. Holler, et al.; Mol. Cell. Biol.
23, 1428 (2003),
Abstract;
Full Text
Death ligand TRAIL induces no apoptosis but inhibits activation of human (auto)antigen-specific T cells: J.D. Lunemann, et al.; J. Immunol.
168, 4881 (2002),
Abstract;
Full Text
Induction of TRAIL-mediated glioma cell death by human T cells: J. Dörr, et al.; J. Neuroimmunol.
122, 117 (2002),
Abstract;
Innate direct anticancer effector function of human immature dendritic cells. II. Role of TNF, lymphotoxin-alpha(1)beta(2), Fas ligand, and TNF-related apoptosis-inducing ligand: G. Lu, et al.; J. Immunol.
168, 1831 (2002),
Abstract;
Full Text
Mitogen-Activated Protein Kinase/Extracellular Signal-Regulated Kinase Signaling in Activated T Cells Abrogates TRAIL-Induced Apoptosis Upstream of the Mitochondrial Amplification Loop and Caspase-8: T.S. Soderstrom, et al.; J. Immunol.
169, 2851 (2002),
Abstract;
T cells require TRAIL for optimal graft-versus-tumor activity: C. Schmaltz, et al.; Nat. Med.
8, 1433 (2002),
Abstract;
TRAIL/Apo-2 ligand induces primary plasma cell apoptosis: J. Ursini-Siegel, et al.; J. Immunol.
169, 5505 (2002),
Abstract;
Full Text
Development of improved soluble inhibitors of FasL and CD40L based on oligomerized receptors: N. Holler, et al.; J. Immunol. Methods
237, 159 (2000),
Abstract;
The tumor necrosis factor-related apoptosis-inducing ligand receptors TRAIL-R1 and TRAIL-R2 have distinct cross-linking requirements for initiation of apoptosis and are non-redundant in JNK activation: F. Mühlenbeck, et al.; J. Biol. Chem.
275, 32208 (2000),
Abstract;
Full Text
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