Recombinant Cynomolgus TNF RI/TNFRSF1A 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 ED50 for this effect is 0.6-3.6 ng/mL.
|
Source |
Human embryonic kidney cell, HEK293-derived cynomolgus monkey TNF RI/TNFRSF1A protein Cynomolgus Monkey TNF RI/TNFRSF1A (Leu30-Thr211) Accession # NP_001306550 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus |
| C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Leu30 |
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 |
47 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 |
55-66 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
- 12 months from date of receipt, ≤ -20 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, ≤ -20 °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 Cynomolgus TNF RI/TNFRSF1A Fc Protein, CF
Background
TNF
receptor 1 is a 55 kDa type I transmembrane protein member of the TNF receptor
superfamily, designated TNFRSF1A (1, 2). TNF RI is a 455 amino acid (aa) protein
that contains a signal sequence and ECD with a PLAD (pre-ligand assembly domain)
that mediates constitutive dimer/trimer formation, followed by four CRD
(cysteine-rich domains), a transmembrane domain, and a cytoplasmic domain
that contains a neutral sphingomyelinase activation domain and a death domain
(3, 4). The ECD of cynomolgus TNF RI shows 97%, 69%, and 68% aa identity with
human, mouse and rat TNF RI, respectively. Both TNF RI and TNF RII (TNFRSF1B)
are widely expressed and contain four TNF-alpha trimer-binding CRD in their
ECD. However, TNF RI is thought to mediate most of the cellular effects of
TNF-alpha (3). TNF RI is essential for proper development of lymph node germinal
centers and Peyer's patches, and for combating intracellular pathogens such as
Listeria (1, 2, 5). TNF RI is also a receptor for TNF-beta/TNFSF1B (lymphotoxin-alpha)
(6). TNF RI is stored in the Golgi and translocates to the cell surface
following pro‑inflammatory
stimuli (7). TNF-alpha stabilizes TNF RI and induces its sequestering in lipid
rafts, where it activates NF kappa B and is cleaved by ADAM-17/TACE (8, 9, 16).
Release of the 28-34 kDa TNF RI ECD also occurs constitutively and in response
to products of pathogens such as LPS, CpG DNA or
S. aureus protein A (1, 10-12). Full-length TNF RI may also be released in exosome-like vesicles (13).
Release helps to resolve inflammatory reactions, since it down-regulates cell
surface TNF RI and provides soluble TNF RI to bind TNF-alpha (10, 14-15).
Exclusion from lipid rafts causes endocytosis of TNF RI complexes and induces
apoptosis (1). Mutations of human TNF R1 can result in inflammatory episodes
known as TRAPS (TNFR-associated periodic syndrome) (7).
- Pfeffer, K. (2003) Cytokine Growth Factor Rev. 14:185.
- Hehlgans, T. and K. Pfeffer (2005) Immunology 115:1.
- Chan, F.K. et al. (2000) Science 288:2351.
- Schall, T.J. et al. (1990) Cell 61:361.
- Peschon, J.J. et al. (1998) J. Immunol. 160:943.
- Banner, D.W et al. (1993) Cell 73:431.
- Turner, M.D. et al. (2012) Biosci. Rep. 32:105.
- Legler, D.F. et al. (2003) Immunity 18:655.
- Tellier, E. et al. (2006) Exp. Cell Res. 312:3969.
- Xanthoulea, S. et al. (2004) J. Exp. Med. 200:367.
- Jin, L. et al. (2000) J. Immunol. 165:5153.
- Gomez, M.I. et al. (2006) J. Biol. Chem. 281:20190.
- Islam, A. et al. (2006) J. Biol. Chem. 281:6860.
- Garton, K.J. et al. (2006) J. Leukoc. Biol. 79:1105.
- McDermott, M.F. et al. (1999) Cell 97:133.
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