Recombinant Mouse DcTRAILR2/TNFRSF22 Protein

• Reactivity: Mu
• Applications: Bioactivity

Recombinant Mouse DcTRAILR2/TNFRSF22 Protein Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Mouse DcTRAIL R2/TNFRSF22 is immobilized at 0.5 μg/mL, the concentration of Recombinant Human TRAIL/TNFSF10 (Catalog # 375-TEC) that produces 50% of the optimal binding response is found to be approximately 20-100 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse DcTRAIL R2/TNFRSF22 protein
  Ala39-Arg175 & Met40-Arg175, both with a C-terminal 10-His tag
• Accession #: Q9ER62
• N-terminal Sequence: Ala39 & Met40
• Protein/Peptide Type: Recombinant Proteins
• Gene: Tnfrsf22
• Purity: >90%, 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: 16.5 kDa.
  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: Multiple bands between 25-33 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 with BSA as a carrier protein.
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse DcTRAILR2/TNFRSF22 Protein

• APO-3;DDR3;DR3;GEF720;LARD;PLEKHG5;TNFRSF12;TNFRSF25;TR3;TRAMP;Tumor necrosis factor receptor superfamily member 25;WSL-1;WSL-LR
• DcTRAIL R2
• DcTRAILR2
• SOBa
• TNFRH2
• TNFRSF22

Background

TRAIL interacts via a complex receptor system to preferentially induce apoptosis of tumor cells in vivo and in vitro (1). In human, two signaling receptors (TRAIL R1 and TRAIL R2) and three decoy receptors (TRAIL R3, TRAIL R4, and OPG) for TRAIL exist. Mouse homologues of human TRAIL R1, -3, and -4 have not been found. Three novel mouse genes (TNF RH1, -2, and -3) that encode proteins with the classic TNF receptor cysteine-rich domains (CRDs) have been identified. These mouse genes are closely clustered on distal mouse chromosome 7 and do not have orthologues in the corresponding human chromosomal region (2). TNF RH1 and -2 have been implicated as decoy receptors for mouse TRAIL and named mDcTRAIL R1/TNFRSF23 and mDcTRAIL R2/TNFRSF22, respectively. The ligand for TNF RH3 is not known (1).

The mouse decoy TRAIL R2 (mDcTRAIL R2) gene encodes a 198 amino acid (aa) residues type I transmembrane protein with a putative 39 aa signal peptide, a 136 aa extracellular domain, a 18 aa transmembrane region, and a 5 aa cytoplasmic tail (1, 2). An alternatively spliced variant encoding a secreted soluble receptor of 180 aa has also been described. The transmembrane and soluble receptors are known as mDcTRAIL R2_L and mDcTRAIL R2_S, respectively. Both mDcTRAIL R2 isoforms and the GPI-linked mDcTRAIL R1 bind TRAIL specifically but are incapable of triggering signal transduction. Mouse DcTRAIL R1 and mDcTRAIL R2 share 71% sequence identity (3). The two receptors have similar structural modules in their CRDs, which differ from those found in the CRDs of mTNF RH3 (2, 3). Mouse DcTRAIL R1 preferentially binds mTRAIL while mDcTRAIL R2 binds both human and mTRAIL. mRNA of mouse DcTRAIL R1 and -2 are expressed at low levels in many mouse tissues and at higher levels in several mouse cell lines.

1. Engemann, S. et al. (2000) Hum. Mol. Genet. 9:2691.
2. Schneider, P. et al. (2003) J. Biol. Chem. 278:5444.
3. Bodmer, J.-L. et al. (2002) Trends Biochem. Sci. 27:19.

Bioinformatics

• Gene Symbol: Tnfrsf22
• Uniprot:
  • Q9ER62()