Recombinant Human TRAILR1/TNFRSF10A Fc Chimera Protein, CF Summary
Additional Information
A New rh TRAIL R1 is Now Available! ~2 fold better activity; CHO expressed; No his tag!
Details of Functionality
Measured by its ability to inhibit TRAIL-mediated cytotoxicity using L‑929 mouse fibroblast cells treated with TRAIL. The ED50 for this effect is 1-3 ng/mL in the presence of 6 ng/mL of Recombinant Human TRAIL/TNFSF10 (Catalog # 375-TEC).
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human TRAIL R1/TNFRSF10A protein
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
43 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
46 kDa, reducing conditions
Publications
Read Publications using 347-DR/CF in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human TRAILR1/TNFRSF10A Fc Chimera Protein, CF
APO2
CD261 antigen
CD261
cytotoxic TRAIL receptor
Death receptor 4
DR4 TRAIL receptor 1
DR4
TNF-related apoptosis inducing ligand receptor 1
TNF-related apoptosis-inducing ligand receptor 1
TNFRSF10A
TRAIL R1
TRAILR1
TRAIL-R1
TRAILR-1
TRAILR1MGC9365
tumor necrosis factor receptor superfamily member 10A
tumor necrosis factor receptor superfamily, member 10a
Background
Human TRAIL R1 (TNF-related apoptosis inducing ligand receptor 1), also called DR4 (death receptor 4), is a 50 ‑ 57 kDa, 468 amino acid (aa) type 1 transmembrane protein in the TNF R family, designated TNFRSF10A (1 ‑ 3). Of the five receptors for TRAIL (also called APO2 ligand) in humans, TRAIL R1/DR4 and TRAIL R2/DR5 are apoptosis-inducing and share 59% aa identity within the cytoplasmic death domain (aa 365 ‑ 448 of human TRAIL R1) (1 ‑ 3). Rodents do not express TRAIL R1/DR4. Human decoy receptors TRAIL R3 and TRAIL R4 have non-functional death domains but share ~60% aa identity with TRAIL R1 within extracellular TNFR domains (aa 107 ‑ 229), while the secreted TRAIL receptor osteoprotegerin shares only 18% aa identity with TRAIL R1. Trimeric TRAIL engagement of TRAIL R1 induces apoptosis by recruiting a cytosolic death-inducing signaling complex (DISC) that includes the adaptor FADD and caspases 8 and 10 (2 ‑ 6). TRAIL R1 translational modifications, such as O-glycosylation and palmitoylation, promote apoptosis by enhancing oligomerization and presence in lipid rafts, respectively (3 ‑ 6). Recombinant human TRAIL R1 neutralizes the ability of TRAIL to induce apoptosis (1). TRAIL R1 protein is expressed mainly in damaged, infected and malignant cells and can be repressed by hedgehog proteins in oncogenic cells (3, 7, 8). TRAIL R1 is also expressed on hemopoietic cells and influences activities such as monocyte migration (9). On senescent neutrophils, CXCL12/SDF-1 engagement of CXCR4 induces expression of all TRAIL R (7). TRAIL functions in immune surveillance, inducing apoptosis in cancer cells but not normal cells (3, 10, 11). TRAIL R1 surface expression correlates more closely than that of TRAIL R2 with TRAIL induction of apoptosis on tumor cells such as melanoma and chronic lymphocytic and acute myeloid leukemias (6, 12, 13).
Pan, G. et al. (1997) Science 276:111.
Zauli, G. and P. Secchiero (2006) Cytokine Growth Factor Rev. 17:245.
Yang, A. et al. (2010) Curr. Opin. Cell Biol. 22:837.
Rossin, A. et al. (2009) Biohem. J. 419:185.
Psahoulia, F.H. et al. (2007) Mol. Cancer Ther. 6:2591.
Ries, C.R. et al. (2010) Cell Death Dis. 1:e83.
Lum, J.J. et al. (2005) J. Immunol. 175:1232.
Kurita, S. et al. (2010) Oncogene 29:4848.
Wei, W. et al. (2010) Mol. Immunol. 47:2475.
Sung, E-S. et al. (2009) Mol. Cancer Ther. 8:2276.
Mom, C.H. et al. (2009) Clin. Cancer Res. 15:5584.
MacFarlane, M. et al. (2005) Cell Death Differ. 12:773.
Kurbanov, B.M. et al. (2005) J. Invest. Dermatol. 125:1010.
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