Recombinant Human TNF RII/TNFRSF1B Fc Chimera Protein, CF


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Product Details

Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human TNF RII/TNFRSF1B Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit the TNF-alpha mediated cytotoxicity in the L‑929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. Matthews, N. and M.L. Neale (1987) in Lymphokines and Interferons, A Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 221. The ED50 for this effect, in the presence of 0.25 ng/mL of TNF-alpha, is 0.004‑0.016 µg/mL.
Mouse myeloma cell line, NS0-derived human TNF RII/TNFRSF1B protein
Accession # AAA36755
6-His tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
>95%, 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.


Theoretical MW
52.6 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.
70 kDa, reducing conditions
Read Publications using
726-R2 in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in PBS.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.


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

Alternate Names for Recombinant Human TNF RII/TNFRSF1B Fc Chimera Protein, CF

  • CD120b antigen
  • CD120b
  • Etanercept
  • p75 TNF receptor
  • p75TBPII
  • p75TNFR
  • soluble TNFR1B variant 1
  • TNFBRp80 TNF-alpha receptor
  • TNF-R2
  • TNF-R75
  • TNFR80
  • TNF-R-II
  • tumor necrosis factor beta receptor
  • tumor necrosis factor binding protein 2
  • Tumor necrosis factor receptor 2
  • tumor necrosis factor receptor superfamily member 1B
  • tumor necrosis factor receptor superfamily, member 1B
  • Tumor necrosis factor receptor type II


Tumor Necrosis Factor Receptor II (TNF RII), also known as TNFRSF1B, p75/p80, and CD120b, is a type I transmembrane protein that belongs to the TNF receptor superfamily. It has a molecular weight of approximately 75 kDa (1-4). The TNF receptor superfamily is comprised of structurally related receptors that bind to TNF-related ligands and regulate numerous processes such as immune cell activation and apoptosis. Receptors in this superfamily are characterized by the presence of a cysteine-rich region in their extracellular domain (ECD) (1-3, 5). Human TNF RII contains four cysteine-rich repeats in its ECD, which shares 58% and 56% amino acid sequence identity with the mouse and rat orthologs, respectively. Several receptors in the TNF superfamily also contain intracellular death domains (DDs) that recruit caspase-interacting proteins to initiate apoptosis upon ligand binding. Those receptors that lack DDs, like TNF RII, bind TNF Receptor-associated Factors, which transduce signals generated by activation of these receptors (6, 7).

TNF RII is expressed predominantly on cells of the hematopoietic lineage, such as T and natural killer cells, as well as on endothelial cells, microglia, astrocytes, neurons, oligodendrocytes, cardiac myocytes, thymocytes, and mesenchymal stem cells (6, 8-10). TNF RII binds to the membrane-bound forms of TNF-alpha and Lymphotoxin-alpha /TNF-beta ; soluble TNF is thought to signal predominately through TNF RI (7, 11). TNF RII activation primarily initiates pro-inflammatory and pro-survival responses via NF kappa B-dependent signaling pathways (6, 7, 12-15). However, under certain conditions, TNF RII signaling can induce apoptosis (6). TNF RII also exists as a soluble receptor, which can be generated by proteolytic cleavage of its ECD from the cell surface or by alternative splicing (2, 16). Soluble TNF RII is believed to inhibit TNF biological activity by binding TNF thereby preventing it from activating membrane TNF receptors (17). Polymorphisms of the human TNFR2 gene, which result in increased expression of both membrane-bound and soluble TNF RII, have been associated with several autoimmune diseases including Crohn’s disease, systemic lupus erythematosus, and familial rheumatoid arthritis (6, 17).

  1. Dembic, Z. et al. (1990) Cytokine 2:231.
  2. Kohno, T. et al. (1990) Proc. Natl. Acad. Sci. USA 87:8331.
  3. Lewis, M. et al. (1991) Proc. Natl. Acad. Sci. USA 88:2830.
  4. Loetscher, H. et al. (1990) J. Biol. Chem. 265:20131.
  5. Beltinger, C.P. et al. (1996) Genomics 35:94.
  6. Faustman, D. and M. Davis (2010) Nat. Rev. Drug Discov. 9:482.
  7. Ihnatko, R. and M. Kubeš (2007) Gen. Physiol. Biophys. 26:159.
  8. Mason, A.T. et al. (1995) J. Leukoc. Biol. 58:249.
  9. Speeckaert, M.M. et al. (2012) Am. J. Nephrol. 36:261.
  10. Böcker, W. et al. (2008) J. Mol. Med. 86:1183.
  11. Pennica, D. et al. (1992) J. Biol. Chem. 267:21172.
  12. Mak, T.W. and W.C. Yeh (2002) Arthritis Res. 4:S243.
  13. Aspalter, R.M. et al. (2003) J. Leukoc. Biol. 74:572.
  14. Bradley, J.R. (2008) J. Pathol. 214:149.
  15. McCoy, M.K. and M.G. Tansey (2008) J. Neuroinflammation 5:45.
  16. Lainez, B. et al. (2004) Int. Immunol. 16:169.
  17. Sennikov, S.V. et al. (2014) Mediators Inflamm. 2014:745909.

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Publications for TNF RII/TNFRSF1B (726-R2)(5)

We have publications tested in 2 confirmed species: Human, N/A.

We have publications tested in 2 applications: Bioassay, ELISA Standard.

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Showing Publications 1 - 5 of 5.
Publications using 726-R2 Applications Species
M Inoue, D Ando, H Kamada, S Taki, M Niiyama, Y Mukai, T Tadokoro, K Maenaka, T Nakayama, Y Kado, T Inoue, Y Tsutsumi, SI Tsunoda A trimeric structural fusion of an antagonistic tumor necrosis factor-? mutant enhances molecular stability and enables facile modification J. Biol. Chem, 2017;0(0):. 2017 [PMID: 28235800] (Bioassay, N/A) Bioassay N/A
Dulos J, van der Vleuten MA, Kavelaars A, Heijnen CJ, Boots AM CYP7B expression and activity in fibroblast-like synoviocytes from patients with rheumatoid arthritis: regulation by proinflammatory cytokines. Arthritis Rheum., 2005;52(3):770-8. 2005 [PMID: 15751070] (Bioassay, Human) Bioassay Human
Jyonouchi H, Sun S, Itokazu N Innate immunity associated with inflammatory responses and cytokine production against common dietary proteins in patients with autism spectrum disorder. Neuropsychobiology, 0;46(2):76-84. 0 [PMID: 12378124] (ELISA Standard, N/A) ELISA Standard N/A
Ryon JJ, Moss WJ, Monze M, Griffin DE Functional and phenotypic changes in circulating lymphocytes from hospitalized zambian children with measles. Clin. Diagn. Lab. Immunol., 2002;9(5):994-1003. 2002 [PMID: 12204949] (Bioassay, Human) Bioassay Human
Bharucha AE, Jorgensen R, Lichtman SN, LaRusso NF, Lindor KD A pilot study of pentoxifylline for the treatment of primary sclerosing cholangitis. Am. J. Gastroenterol., 2000;95(9):2338-42. 2000 [PMID: 11007239] (ELISA Standard, N/A) ELISA Standard N/A

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Gene Symbol TNFRSF1B