Recombinant Cynomolgus TNF RII/TNFRSF1B Fc 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 ED 50 for this effect is 0.2-1.2 ng/mL in the presence of 0.25 ng/mL of Recombinant Human TNF-alpha
(Catalog #
210-TA). |
Source |
Chinese Hamster Ovary cell line, CHO-derived cynomolgus monkey TNF RII/TNFRSF1B protein Cynomolgus Monkey TNF RII/TNFRSF1B (Leu23-Asp257) Accession # XP_005544817.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Leu23 |
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 |
|
Theoretical MW |
36 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 |
68-80 kDa, under 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 Trehalose. |
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 Cynomolgus TNF RII/TNFRSF1B Fc Protein, CF
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 (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). Cynomolgus monkey TNF RII shares 97% sequence identity in the ECD
with its human homolog. 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, and thymocytes (6, 8, 9). TNF RII activation primarily
initiates pro-inflammatory and pro-survival responses via NF kappa B-dependent
signaling pathways (6, 7). However, under certain conditions, TNF RII signaling
can induce apoptosis (8). Soluble TNF RII is believed to inhibit TNF biological
activity by binding TNF thereby preventing it from activating membrane TNF
receptors (10).
- 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.
- Sennikov, S.V. et al. (2014) Mediators Inflamm. 2014:745909.
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