Recombinant Mouse TNF RII/TNFRSF1B Fc Chimera Protein, CF

Recombinant Mouse TNF RII/TNFRSF1B (Catalog # 9707‑R2)inhibits Recombinant Mouse TNF‑alpha aa 80‑235 (Catalog # 410‑MT) mediated cytotoxicity inthe L‑929mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. The ED50 for this effect is 3‑15 ng/mL.

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

Recombinant Mouse 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 is 3-15 ng/mL
• Source: Mouse myeloma cell line, NS0-derived mouse TNF RII/TNFRSF1B protein
  

  Mouse TNF RII/TNFRSF1B (Val23-Gly258) Accession # P25119	IEGRMDP	Mouse IgG2a (Glu98-Lys330)
  N-terminus		C-terminus

• Accession #: P25119
• N-terminal Sequence: Val23
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 52 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: 66-76 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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Mouse 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

Two types of soluble TNF receptors have been identified in human serum and urine which can neutralize the biological activities of TNF-alpha and TNF-beta (1, 2). These binding proteins represent truncated forms of the two types of high-affinity cell surface receptors for TNF (TNFR-p60 Type B and TNFR-p80 Type A). Soluble TNF RII corresponds to TNFR-p80 Type A (3). In the new TNF superfamily nomenclature, TNF RII is referred to as TNFRSF1B. These apparent soluble forms of the receptors appear to arise as a result of shedding of the extracellular domains of the membrane-bound receptors. Normal concentrations as high as 4 ng/mL are found in the serum of healthy individuals, and even higher levels may be found in some pathological conditions (4). Mature mouse TNF RII contains an extracellular domain (ECD, aa 23 - 258) containing ten disulfide bonds, a transmembrane domain (aa 259-288), and a cytoplasmic domain (aa 289-474). Within the ECD, the mouse TNF RII shares 57% and 84% aa sequence identity to human and rat TNF RII. 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, and thymocytes (5-7). TNF RII activation primarily initiates pro-inflammatory and pro-survival responses via NF kappa B-dependent signaling pathways (5, 8). However, under certain conditions, TNF RII signaling can induce apoptosis (5). Soluble TNF RII is believed to inhibit TNF biological activity by binding TNF thereby preventing it from activating membrane TNF receptors (9).

1. Smith, C.A. et al. (1990) Science 248: 1019.
2. Goodwin R.G. et al. (1991) Mol. Cell. Biol. 11:3020.
3. Kohno, T. et al. (1990) Proc. Natl. Acad. Sci. USA 87:8331.
4. Yamada, Y. et al. (2000) Burns 26:239.
5. Faustman, D. and M. Davis (2010) Nat. Rev. Drug Discov. 9:482.
6. Mason, A.T. et al. (1995) J. Leukoc. Biol. 58:249.
7. Speeckaert, M.M. et al. (2012) Am. J. Nephrol. 36:261.
8. Ihnatko, R. and M. Kubeš (2007) Gen. Physiol. Biophys. 26:159.
9. Sennikov, S.V. et al. (2014) Mediators Inflamm. 2014:745909.

Publications for TNF RII/TNFRSF1B (9707-R2)(2)

Publications using 9707-R2

• Inoue, M;Tsuji, Y;Ueno, R;Miyamoto, D;Tanaka, K;Moriyasu, Y;Shibata, S;Okuda, M;Ando, D;Abe, Y;Kamada, H;Tsunoda, SI; Bivalent structure of a TNFR2-selective and agonistic TNF-? mutein Fc-fusion protein enhances the expansion activity of regulatory T cells Scientific reports 2023-08-23 [PMID: 37612373] (Bioassay, N/A)
• T Kurosawa, M Goto, N Kaji, S Aikiyo, T Mihara, M Ikemoto-Ue, M Toyoda, N Kanazawa, T Nakazawa, M Hori, A Uezumi Liver fibrosis-induced muscle atrophy is mediated by elevated levels of circulating TNF&amp;alpha Cell Death & Disease, 2021-01-07;12(1):11. 2021-01-07 [PMID: 33414474] (Bioassay, Mouse)

Bioinformatics

• Uniprot:
  • P25119()