• Purity

  >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie? Blue Staining

• Endotoxin Level

  <1.0 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its binding ability in a functional ELISA. When Recombinant Human TL1A/TNFSF15 (Catalog # /CF) is immobilized at 2 μg/mL (100 μL/well), the concentration of Recombinant Human DR3/TNFRSF25 Fc Chimera that produces 50% of optimal binding response is approximately 0.5-2.5 μg/mL.

• Source

  Mouse myeloma cell line, NS0-derived

  Human DR3 (Gln25-Phe201) & (Arg29-Phe201) Accession # Q93038.2	IEGRMD	Human IgG1 (Pro100-Lys330)	6-His tag
  N-terminus			C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Arg29 & No results obtained: Gln25 predicted    
   

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  46.6 kDa (monomer)

• SDS-PAGE

  50-65 kDa, reducing conditions

Background: DR3/TNFRSF25

Death receptor 3 (DR3), also known as lymphocyte-associated receptor of death (LARD), WSL-1, APO3, TRAMP and TR3, is a glycoprotein belonging to the TNF receptor superfamily (TNFRSF) (1 - 5). DR3 was formerly designated TNFRSF12 when it was thought to be a receptor for TWEAK/TNFSF12 (6). However, work disavowed the DR3:TWEAK interaction and DR3 is now designated TNFRSF 25 (7). By alternative splicing, at least 11 distinct human DR3 transcripts encoding secreted or type I membrane proteins exist (7). The human DR3 isoform 1 cDNA encodes a 417 amino acid residue (aa) transmembrane precursor with a 24 aa signal peptide, a 175 aa extracellular domain containing four cysteine-rich repeats and two potential N-glycosylation sites, a 21 aa transmembrane region and a 195 aa cytoplasmic region with one death domain. DR3 is one of six within the TNF R superfamily that contains a death domain in its cytooplasmic region. It is most closely related to TNF R1 and FAS/CD95, sharing 29% and 23% aa sequence identity, respectively. DR3 is expressed primarily in tissues enriched in lymphocytes. Whereas na?ve B and T cells express multiple truncated DR3 isoforms but not the transmembrane isoform 1, upon T cell activation, expression of the transmembrane DR3 isoform 1 predominates. TL1A/VEGI, a TNF superfamily ligand, has been shown to bind and activate DR3 (8). Depending on the cell context, ligation of DR3 by TL1A can trigger one of two signaling pathways. On primary T cells, TL1A induces NF-kappa-B activation and a costimulatory signal to increase IL-2 responsiveness and the secretion of proinflammatory cytokines. However, in a tumor cell line, TF-1, TL1A has been shown to induce caspase activity and apoptosis. In DR3-null mice, an impairment of negative selection and anti-CD3-mediated thymocyte apoptosis is observed.

• References:

1. Chinnaiyan, A.M., et al. (1996) Science 274:990.

2. Kitson, J., et al. (1996) Nature 384:372.

3. Bodmer, J-L., et al. (1997) Immunity 6:79.

4. Screaton, G.R. et al. (1997) Proc. Nat. Acad. Sci. USA 94:4615.

5. Marsters, S.A. et al. (1996) Curr. Biol. 6:1669.

6. Marsters, S.A. et al. (1998) Curr. Biol. 8:525.

7. Kaptein, A. et al. (2000) FEBS Lett. 485:135.

8. Migone, T-S. et al. (2002) Immunity 16:479.

• Long Name:

  Death Receptor 3

• Entrez Gene IDs:

  8718 (Human); 85030 (Mouse)

• Alternate Names:

  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