Recombinant Canine TNF RI/TNFRSF1A Protein Summary
Product Specifications
Ile22-Thr211, with an N-terminal Met
Analysis
Product Datasheets
4017-TR (with carrier)
4017-TR/CF (carrier free)
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
4017-TR
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Reconstitution | Reconstitute at 10 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
4017-TR/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: TNF RI/TNFRSF1A
TNF receptor 1 (TNF RI; also called TNF R-p55/p60, TNFRSF1A and CD120a) is a type I transmembrane protein that belongs to the TNF receptor superfamily (1, 2). TNF RI is widely expressed and is present on the cell surface as a trimer of 55 kDa subunits. It serves as a receptor for both TNF-alpha and TNF-beta /lymphotoxin. Each subunit contains four TNF-alpha trimer-binding cysteine-rich domains (CRD) in its extracellular domain (ECD) (1 - 6). TNF-alpha binding to TNF R1 induces the sequestration of TNF RI in lipid rafts, where it activates NF kappa B and is cleaved by ADAM-17/TACE (7, 8). Release of the 28 - 34 kDa TNF RI ECD occurs constitutively, and in response to products of pathogens such as LPS, CpG DNA or S. aureus protein A (1, 7 - 12). Full-length TNF RI may also be released in exosome-like vesicles (12). This release helps to resolve inflammatory reactions as it down-regulates cell surface TNF RI and provides soluble TNF RI to bind TNF-alpha (6, 13, 14). Exclusion from lipid rafts causes endocytosis of TNF RI complexes and induces apoptosis (7, 15). Although there is a second receptor for TNF-alpha (TNF R2), TNF RI is thought to mediate most of the cellular effects of TNF-alpha (3). TNF R1 is essential for proper development of lymph node germinal centers and Peyer’s patches, and for combating intracellular pathogens such as Listeria monocytogenes (1 - 3). Canine TNF RI is a 452 amino acid (aa) protein (16). Based on human, its ECD will contain a PLAD domain that mediates constitutive trimer formation (6). The PLAD domain will be followed by four CRDs, a transmembrane domain, and a cytoplasmic sequence that contains a neutral sphingomyelinase activation domain and a death domain. The ECD of canine TNF RI shows approximately 87%, 75%, 80%, 66% and 67% aa identity with feline, porcine, human, rat and mouse TNF RI, respectively.
- Pfeffer, K. (2003) Cytokine Growth Factor Rev. 14:185.
- Hehlgans, T. and K. Pfeffer (2005) Immunology 115:1.
- Peschon, J.J. et al. (1998) J. Immunol. 160:943.
- Banner, D.W et al. (1993) Cell 73: 431.
- Medvedev, A.E. et al. (1996) J. Biol. Chem. 271:9778.
- Chan, F.K. et al. (2000) Science 288:2351.
- 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.
- Schneider-Brachert, W. et al. (2004) Immunity 21:415.
- GenBank Accession # XP_854474.
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