Recombinant Human TNF RII/TNFRSF1B Fc Chimera Protein, CF
R&D Systems, part of Bio-Techne | Catalog # 726-R2
Key Product Details
Source
Accession #
Structure / Form
Conjugate
Applications
Product Specifications
Source
Human TNF RII (Leu23-Asp257) Accession # AAA36755 |
IEGRMD | Human IgG1 (Pro100-Lys330) |
6-His tag |
N-terminus | C-terminus |
Purity
Endotoxin Level
N-terminal Sequence Analysis
Predicted Molecular Mass
SDS-PAGE
Activity
The ED50 for this effect, in the presence of 0.25 ng/mL of TNF-alpha, is 0.004-0.016 µg/mL.
Formulation, Preparation and Storage
726-R2
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution |
Reconstitute at 100 μg/mL in sterile PBS.
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Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Background: TNF RII/TNFRSF1B
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 kappaB-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).
References
- Dembic, Z. et al. (1990) Cytokine 2:231.
- Kohno, T. et al. (1990) Proc. Natl. Acad. Sci. USA 87:8331.
- Lewis, M. et al. (1991) Proc. Natl. Acad. Sci. USA 88:2830.
- Loetscher, H. et al. (1990) J. Biol. Chem. 265:20131.
- Beltinger, C.P. et al. (1996) Genomics 35:94.
- Faustman, D. and M. Davis (2010) Nat. Rev. Drug Discov. 9:482.
- Ihnatko, R. and M. Kubeš (2007) Gen. Physiol. Biophys. 26:159.
- Mason, A.T. et al. (1995) J. Leukoc. Biol. 58:249.
- Speeckaert, M.M. et al. (2012) Am. J. Nephrol. 36:261.
- Böcker, W. et al. (2008) J. Mol. Med. 86:1183.
- Pennica, D. et al. (1992) J. Biol. Chem. 267:21172.
- Mak, T.W. and W.C. Yeh (2002) Arthritis Res. 4:S243.
- Aspalter, R.M. et al. (2003) J. Leukoc. Biol. 74:572.
- Bradley, J.R. (2008) J. Pathol. 214:149.
- McCoy, M.K. and M.G. Tansey (2008) J. Neuroinflammation 5:45.
- Lainez, B. et al. (2004) Int. Immunol. 16:169.
- Sennikov, S.V. et al. (2014) Mediators Inflamm. 2014:745909.
Long Name
Alternate Names
Gene Symbol
UniProt
Additional TNF RII/TNFRSF1B Products
Product Documents for Recombinant Human TNF RII/TNFRSF1B Fc Chimera Protein, CF
Product Specific Notices for Recombinant Human TNF RII/TNFRSF1B Fc Chimera Protein, CF
For research use only