Product Pathways - NF-kB Signaling
A20/TNFAIP3 Antibody #4625
|4625S||100 µl (10 western blots)||---||In Stock||---|
|4625||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
A20/TNFAIP3 Antibody detects endogenous levels of total A20/TNFAIP3 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly267 of human A20/TNFAIP3. Antibodies were purified by protein A and peptide affinity chromatography.
A20, also referred to as TNF-α-induced protein 3 (TNFAIP3), is cytokine-inducible protein that functions to inhibit apoptosis and activate NF-κB (1,2). It was first identified as a TNF-α inducible primary response gene in human umbilical vein endothelial cells, and encodes a 790-amino acid protein containing seven Cys2/Cys2-zinc finger motifs (3). Constitutive expression of A20 is observed in lymphoid tissues (4), but it is transiently expressed in a variety of cell types in response to inflammatory signals such as TNF-α (3,5), IL-1 (3,5), phorbol esters (6), and LPS (7). Expression of A20 can confer resistance to apoptosis and NF-κB activation triggered by these signals, probably through interference with TRAF (TNF receptor associated factor) family members (8,9), and interaction with the NF-κB inhibiting protein ABIN (10). Studies also show that A20 contains site-specific ubiquitin modifying activity that can contribute to its biological functions (11,12). The amino-terminus of A20 contains de-ubiquitinating (DUB) activity for Lys63 branches, such as those found in TRAF6 and RIP, while the carboxyl-terminus contains ubiquitin ligase (E3) activity for Lys48 branches of the same substrates and leads to their degradation (12).
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- Lee, E.G. et al. (2000) Science 289, 2350-4.
- Dixit, V.M. et al. (1990) J Biol Chem 265, 2973-8.
- Tewari, M. et al. (1995) J Immunol 154, 1699-706.
- Jäättelä, M. et al. (1996) J Immunol 156, 1166-73.
- Laherty, C.D. et al. (1993) J Biol Chem 268, 5032-9.
- Hu, X. et al. (1998) Blood 92, 2759-65.
- Song, H.Y. et al. (1996) Proc Natl Acad Sci USA 93, 6721-5.
- Heyninck, K. and Beyaert, R. (1999) FEBS Lett 442, 147-50.
- Heyninck, K. et al. (1999) J Cell Biol 145, 1471-82.
- Evans, P.C. et al. (2004) Biochem J 378, 727-34.
- Lin, S.C. et al. (2008) J Mol Biol 376, 526-40.
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