|Application ||WB, IHC|
|Calculated MW||89614 Da|
|Other Names||Tumor necrosis factor alpha-induced protein 3, TNF alpha-induced protein 3, 632-, OTU domain-containing protein 7C, Putative DNA-binding protein A20, Zinc finger protein A20, A20p50, A20p37, TNFAIP3, OTUD7C|
|Target/Specificity||A synthetic peptide corresponding to residues in human TNFAIP3 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||TNFAIP3 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquitinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquitinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system. Required for LPS- induced production of proinflammatory cytokines and IFN beta in LPS-tolerized macrophages.|
|Cellular Location||Cytoplasm. Nucleus. Lysosome.|
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Provided below are standard protocols that you may find useful for product applications.
Tumor necrosis factor, alpha-induced protein 3 (TNFAIP3) is a de-ubiquitinating enzyme that contains an N-terminal catalytic domain belonging to the ovarian-tumour superfamily of cysteine proteases (1). TNFAIP3 suppresses apoptosis. It is expressed in various cell types in response to a variety of stimuli that activate the transcription factor NF-kB, including Il-1, CD40 ligand, and PMA (3). TNFAIP3 has been strongly suggested as a key protein involved in tamoxifen resistance, and thus represents both a new breast cancer marker and a promising target for developing new strategies to prevent the emergence of acquired mechanisms of drug resistance in breast cancer (2).
1. Evans P.C., et al. Biochem. J. 378:727-734, 2004 2. Vendrell JA, et al. Oncogene 26(32):4656-67, 2007 3. Daniel S., et al. Blood 104(8):2376-84, 2004
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