Product Pathways - NF-kB Signaling
TNF-R2 Antibody #3727
|3727S||100 µl (10 western blots)||---||In Stock||---|
|3727||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat||Endogenous||65||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Species predicted to react based on 100% sequence homology: Monkey.
Specificity / Sensitivity
TNF-R2 Antibody detects endogenous levels of total TNF-R2 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asp339 within the intracellular region of human TNF-R2. Antibodies are purified by protein A and peptide affinity chromatography.
TNF-α is an important cytokine produced by numerous cell types including neutrophils, activated lymphoctyes, macrophages and NK cells. It plays a critical role in inflammatory responses and in apoptosis (1). TNF-α exists as a membrane-anchored and soluble form, both of which show biological activity. Response to TNF-α is mediated through two receptors, TNF-R1, which is widely expressed, and TNF-R2, which is expressed mainly in immune and endothelial cells (2). Antagonists to TNF-α have been validated as therapeutic targets for rheumatoid arthritis and other immune disorders (3).
The two receptors for TNF-α, TNF-R1 (55 kDa) and TNF-R2 (75 kDa) can mediate distinct cellular responses (4,5). In most cases cytotoxicity elicited by TNF has been reported to act throught TNF-R1 (6,7). In contrast, TNF-R2 appears to be important in T cell signaling and responses to infection (7,8). TNF-R2 binds to distinct members of the TRAF family leading to the activation of NF-κB (9,10). Soluble forms of both receptors have also been characterized which can bind TNF-α and may play an important role in immune disorders (11,12).
- Aggarwal, B.B. (2003) Nat Rev Immunol 3, 745-56.
- Locksley, R.M. et al. (2001) Cell 104, 487-501.
- Taylor, P.C. et al. (2004) Curr Opin Biotechnol 15, 557-63.
- Tartaglia, L.A. et al. (1991) Proc. Natl. Acad. Sci. USA 88, 9292-9296.
- Peschon, J.J. et al. (1998) J. Immunol. 160, 943-952.
- Tartaglia, L.A. et al. (1993) Cell 73, 213-216.
- Rothe, J. et al. (1993) Nature 364, 798-802.
- Aspalter, R.M. et al. (2003) J. Leukoc. Biol. 74, 572-582.
- Rothe, M. et al. (1994) Cell 78, 681-692.
- Rothe, M. et al. (1995) Science 269, 1424-1427.
- Humbert, M. et al. (1994) Am. J. Respir. Crit. Care Med. 149, 1681-1685.
- Schröder, J. et al. (1995) Infection 23, 143-8.
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