Recombinant Human TNF RII/TNFRSF1B Fc Chimera Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

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

• Additional Information: His-tag
• 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.
• Source: Mouse myeloma cell line, NS0-derived human TNF RII/TNFRSF1B protein
  

  Human TNF RII (Leu23-Asp257) Accession # AAA36755	IEGRMD	Human IgG1 (Pro100-Lys330)	6-His tag
  N-terminus			C-terminus

• Accession #: AAA36755
• N-terminal Sequence: Leu23
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: TNFRSF1B
• Purity: >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.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• 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.
• SDS-PAGE: 70 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: >95%, 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 TNF RII/TNFRSF1B Fc Chimera Protein, CF

• CD120b antigen
• CD120b
• Etanercept
• p75 TNF receptor
• p75TBPII
• p75TNFR
• soluble TNFR1B variant 1
• TNF RII
• TNFBRp80 TNF-alpha receptor
• TNF-R2
• TNFR2TNFR1B
• TNF-R75
• TNFR80
• TNFRII
• TNF-RII
• TNF-R-II
• TNFR-II
• TNFRSF1B
• 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

Background

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.

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

Publications using 726-R2

• 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, 2017-02-24;0(0):. 2017-02-24 [PMID: 28235800] (Bioassay)
• 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., 2005-03-01;52(3):770-8. 2005-03-01 [PMID: 15751070] (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, 2002-01-01;46(2):76-84. 2002-01-01 [PMID: 12378124] (ELISA (Standard))
• 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., 2002-09-01;9(5):994-1003. 2002-09-01 [PMID: 12204949] (Bioassay, Human)
• Bharucha AE, 2019, Jorgensen R, Lichtman SN, LaRusso NF, Lindor KD A pilot study of pentoxifylline for the treatment of primary sclerosing cholangitis. 2000-09-01;95(9):2338-42. 2000-09-01 [PMID: 11007239] (ELISA (Standard))

Bioinformatics

• Gene Symbol: TNFRSF1B
• Uniprot:
  • AAA36755()