Recombinant Mouse DR3/TNFRSF25 Fc Chimera Protein, CF

• Reactivity: Mu
• Applications: Binding Activity
• Format: Carrier-Free

Recombinant Mouse DR3/TNFRSF25 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Mouse TL1A/TNFSF15 (Catalog # 1896-TL/CF) is immobilized at 1 μg/mL (100 μL/well), the concentration of Recombinant Mouse DR3/TNFRSF25 Fc Chimera that produces 50% of the optimal binding response is approximately 0.75-4 μg/mL
• Source: Mouse myeloma cell line, NS0-derived mouse DR3/TNFRSF25 protein
  

  Mouse DR3 (Gln31-Phe199) Accession # AAK11256	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: AAK11256
• N-terminal Sequence: No results obtained: Gln31 predicted
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Tnfrsf25
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.1 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 44.6 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: 55-65 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: 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: >90%, 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 Mouse DR3/TNFRSF25 Fc Chimera Protein, CF

• APO3
• Apo-3
• Apoptosis-inducing receptor AIR
• Apoptosis-mediating receptor DR3
• Apoptosis-mediating receptor TRAMP
• Death receptor 3
• DR3
• DR3member 12 (translocatingchain-association membrane protein)
• LARD
• Lymphocyte-associated receptor of death
• Protein WSL
• Protein WSL-1
• TNFRSF25
• TRAMP
• tumor necrosis factor receptor superfamily, member 25
• WSL
• WSL1
• WSL-1

Background

Death receptor 3 (DR3), also known as TNFRSF25, LARD, WSL-1, APO3, TRAMP, and TR3, is a 55 kDa TNF receptor superfamily protein that is predominantly expressed by lymphocytes. TNF receptor superfamily members have varying numbers of extracellular cysteine-rich domains (CRDs) with conserved cysteine spacing (1, 2). DR3 contains four CRDs and one cytoplasmic death domain (3, 4). Alternative splicing of mouse DR3 generates an isoform that lacks the fourth CRD and a secreted isoform that consisits of only the extracellular domain (ECD) (3). Human DR3 exists in at least eleven alternate splice forms (5). Within the ECD, mouse and human DR3 share 59% amino acid (aa) sequence identity. DR3 shares 20%-28% aa sequence identity with the ECD of death domain receptors DR5, DR6, EDAR, Fas, NGF R, and TNF RI. Naïve B and T cells preferentially express truncated soluble isoforms of DR3, whereas stimulated lymphocytes preferentially express transmembrane DR3 (5). TL1A/TNFSF15, a high affinity DR3 ligand which also exists in membrane bound and soluble forms, is expressed by activated endothelial cells and T cells (6, 7). TL1A additionally binds to DcR3/TNFRSF6B, a soluble decoy receptor that interferes with DR3 activation (8). DR3 signaling triggers either apoptosis or NF kappa B-induced anti-apoptotic effects depending on the cellular setting (9). Apoptosis is partially impaired during negative selection of thymocytes in DR3-null mice (10). TL1A interactions with DR3 augment T cell proliferation and proinflammatory cytokine secretion (6, 7, 11, 12). DR3 is upregulated by inflammatory stimulation of CCR9⁺ T cells, a T cell subset important in mucosal immunity (11). T cell and macrophage DR3 expression is prominent in several inflammatory disorders such as Crohn’s disease, inflammatory bowel disease, and atherosclerosis (7, 11-15). DR3 activation on IFN-gamma treated THP-1 cells induces the production of TNF-alpha , CXCL8, CCL2, MMP-1, -9, and -13 (14, 15).

1. Fas, S.C. et al. (2006) Curr. Dir. Autoimmun. 9:1.
2. Aggarwal, B.B. (2003) Nat. Rev. Immunol. 3:745.
3. Wang, E.C.Y. et al. (2001) Immunogenetics 53:59.
4. Borysenko, C.W. et al. (2005) Biochem. Biophys. Res. Commun. 328:794.
5. Screaton, G.R. et al. (1997) Proc. Natl. Acad. Sci. USA 94:4615.
6. Migone, T.S. et al. (2002) Immunity 16:479.
7. Prehn, J.L. et al. (2004) Clin. Immunol. 112:66.
8. Yang, C.-R. et al. (2004) Cancer Res. 64:1122.
9. Wen, L. et al. (2003) J. Biol. Chem. 278:39251.
10. Wang, E.C.Y. et al. (2001) Mol. Cell. Biol. 21:3451.
11. Papadakis, K.A. et al. (2005) J. Immunol. 174:4985.
12. Papadakis, K.A. et al. (2004) J. Immunol. 172:7002.
13. Bamias, G. et al. (2003) J. Immunol. 171:4868.
14. Kim, S.-H. et al. (2001) Jpn. Circ. J. 65:136.
15. Kang, Y.-J. et al. (2005) Cytokine 29:229.

Bioinformatics

• Gene Symbol: Tnfrsf25
• Uniprot:
  • AAK11256()