Recombinant Rat TNF RI/TNFRSF1A 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 0.5-3 ng/mL in the presence of 0.1 ng/mL of Recombinant Rat TNF‑ alpha (Catalog # 510-RT).
Source
Mouse myeloma cell line, NS0-derived rat TNF RI/TNFRSF1A protein
Rat TNF RI/TNFRSF1A (Leu30-Ala211) Accession # P22934
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
47.3 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
60-65 kDa, reducing conditions
Publications
Read Publication using 7990-TR in the following applications:
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 with silver staining
Reconstitution Instructions
Reconstitute at 100 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 Rat TNF RI/TNFRSF1A Fc Chimera Protein, CF
CD120a antigen
CD120a
FPF
p55
p55-R
p60
TNF RI
TNFARMGC19588
TNF-R
TNF-R1
TNFR1TBP1
TNFR55
TNF-R55
TNFR60
TNFRI
TNF-RI
TNF-R-I
TNFR-I
TNFRSF1A
tumor necrosis factor binding protein 1
Tumor necrosis factor receptor 1
tumor necrosis factor receptor 1A isoform beta
tumor necrosis factor receptor superfamily member 1A
tumor necrosis factor receptor superfamily, member 1A
tumor necrosis factor receptor type 1
Tumor necrosis factor receptor type I
tumor necrosis factor-alpha receptor
Background
TNF receptor 1 (TNF RI; also called TNF R‑p55/p60 and TNFRSF1A) is a 55 kDa type I transmembrane protein member of the TNF receptor superfamily, designated TNFRSF1A (1, 2). Rat TNF RI is a 461 amino acid (aa) protein that contains a 21 aa signal sequence, a 190 aa extracellular domain (ECD) with a PLAD (pre‑ligand assembly domain) that mediates constitutive dimer/trimer formation, followed by four CRD (cysteine-rich domains), a 23 aa transmembrane domain, and a 227 aa cytoplasmic sequence that contains a neutral sphingomyelinase activation domain and a death domain (3, 4). The ECD of rat TNF RI shares 69%, 88%, 66%, 68% and 75% aa sequence identity with human, mouse, canine, feline and porcine 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). It 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).
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