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Viral proteins aim to subvert TRAF3 antiviral action.
Mechanistic studies showed that HACE1 (show HACE1 ELISA Kits) exerts its inhibitory role on virus-induced signaling by disrupting the MAVS (show MAVS ELISA Kits)-TRAF3 complex.
An important B cell-sp (show TNFRSF1A ELISA Kits)ecific role for TNFR-associated factor 3 is the (show TNFRSF1A ELISA Kits) inhibition of homeostatic s (show TLR4 ELISA Kits)urvival, directly relevant to the common occurrence of TNFR- (show TNFRSF1A ELISA Kits)associated factor 3 mutations in human B cell malignancies. Review.
The current investigations identified a subset of HPV-positive HNSCCs with mutations in the genes TRAF3 (tumor necrosis factor (show TNF ELISA Kits) receptor-associated factor 3) and CYLD (show CYLD ELISA Kits) (cylindromatosis lysine 63 deubiquitinase). Defects in TRAF3 and CYLD (show CYLD ELISA Kits) correlated with the activation of transcriptional factor nuclear factor kappaB, episomal HPV status of tumors, and improved patient survival.
NDR1 interacts with TRAF3 and interferes with the association of TRAF3 and IL-17R, resulting in increased formation of the activation complex IL-17R-Act1, which is required for the downstream signaling and production of pro-inflammatory factors
Data suggest that UBR5 (show UBR5 ELISA Kits) down-regulates levels of TRAF3, a key component of Toll (show TLR4 ELISA Kits)-like receptor signaling, via the miRNA pathway; p90RSK (show RPS6KA1 ELISA Kits) is an upstream regulator of UBR5 (show UBR5 ELISA Kits); p90RSK (show RPS6KA1 ELISA Kits) phosphorylates UBR5 (show UBR5 ELISA Kits) as required for translational repression of TRAF3 mRNA. (UBR5 (show UBR5 ELISA Kits) = ubiquitin protein ligase E3 component n-recognin 5 (show UBR5 ELISA Kits) protein; TRAF3 = TNF receptor-associated factor 3; p90RSK (show RPS6KA1 ELISA Kits) = 90 kDa ribosomal protein S6 (show RPS6 ELISA Kits) kinase (show RPS6KB1 ELISA Kits))
The GA genotype and GA+AA genotype of TRAF3 rs12147254 were found to increase the risk of coronary heart disease among T2DM patients. the GACGAC haplotype in TRAF3 had a protective effect on T2DM micro-macrovascular complications.
These data suggest an interplay between CELF2 (show CELF2 ELISA Kits) and hnRNP C as the mechanistic basis for activation-dependent alternative splicing of TRAF3 exon 8.
DDX3 (show DDX3X ELISA Kits) directly regulates TRAF3 ubiquitination and acts as a scaffold to co-ordinate assembly of signaling complexes downstream from MAVS (show MAVS ELISA Kits).
The NleB effector limited host IFN-beta (show IFNB1 ELISA Kits) production by inhibiting Lys (show LYZ ELISA Kits)(63)-linked ubiquitination of TNF receptor-associated factor 3 (TRAF3). Inhibition was dependent on the glycosyltransferase activity of NleB.
Depletion of LAP1 during early embryonic myogenesis leads to growth retardation and premature death.
In B lymphocytes, TNFR (show TNFRSF1A ELISA Kits)-associated factor 3 inhibits signaling by TNFR (show TNFRSF1A ELISA Kits) superfamily receptors, Toll (show TLR4 ELISA Kits)-like receptors, and interleukin-6R. In T lymphocytes, TNFR (show TNFRSF1A ELISA Kits)-associated factor 3 is required for normal signaling by the T cell antigen receptor, while inhibiting signaling by the interleukin-2 (show IL2 ELISA Kits) receptor. Cytoplasmic TNFR (show TNFRSF1A ELISA Kits) -associated factor 3 restrains nuclear factor-kappaB2 activation in both T and B cells. Review.
TRAF3 may likely induce apoptosis and resistance to proliferation and may be a new target to inhibit the cyst formation in polycystic kidney disease by regulating the NF-kappaB (show NFKB1 ELISA Kits) signaling pathway Bcl-2 (show BCL2 ELISA Kits) and Bcl-xl (show BCL2L1 ELISA Kits) activity.
this study shows that TRAF3 ubiquitination triggers expulsion of intracellular bacteria by exocyst complex
Data (including data from studies using knockout mice) suggest that RANKL (show TNFSF11 ELISA Kits) enhances TNF (show TNF ELISA Kits)-induced osteoclast formation from precursor spleen cells and enhances bone resorption independently of Traf6 (show TRAF6 ELISA Kits) by degrading Traf3, a known inhibitor of osteoclastogenesis. (RANKL (show TNFSF11 ELISA Kits) = osteoclast differentiation factor (show TNFSF11 ELISA Kits); TNF (show TNF ELISA Kits) = tumor necrosis factor (show TNF ELISA Kits); Traf (show TRAF1 ELISA Kits) = TNF (show TNF ELISA Kits) receptor-associated factor)
Upon stimulation with poly(I:C), malaria parasite-infected red blood cells (iRBCs), or vesicular stomatitis virus (VSV), FOSL1 (show FOSL1 ELISA Kits) "translocated" from the nucleus to the cytoplasm, where it inhibited the interactions between TNF receptor-associated factor 3 (TRAF3), TIR domain-containing adapter inducing IFN-beta (show IFNB1 ELISA Kits) (TRIF (show RNF138 ELISA Kits)), and Tank-binding kinase 1 (TBK1 (show TBK1 ELISA Kits)) via impairing K63-linked polyubiquitination of TRAF3 and TRIF (show RNF138 ELISA Kits).
These findings reveal a novel mechanism that endotoxin tolerance reprograms mitogen-activated protein kinase (show MAPK1 ELISA Kits) signaling by suppressing Pellino 1 (show PELI1 ELISA Kits)-mediated K63-linked ubiquitination of cIAP2 (show BIRC3 ELISA Kits), K48-linked ubiquitination, and degradation of TRAF3.
Findings establish CK1varepsilon as a regulator of antiviral innate immune responses and indicate a novel mechanism of immunoregulation that involves CK1varepsilon-mediated phosphorylation of TRAF3.
Hepatocyte TRAF3 promotes liver steatosis and insulin (show INS ELISA Kits) resistance through targeting TAK1 (show NR2C2 ELISA Kits)-dependent signaling.
The protein encoded by this gene is a member of the TNF receptor associated factor (TRAF) protein family. TRAF proteins associate with, and mediate the signal transduction from, members of the TNF receptor (TNFR) superfamily. This protein participates in the signal transduction of CD40, a TNFR family member important for the activation of the immune response. This protein is found to be a critical component of the lymphotoxin-beta receptor (LTbetaR) signaling complex, which induces NF-kappaB activation and cell death initiated by LTbeta ligation. Epstein-Barr virus encoded latent infection membrane protein-1 (LMP1) can interact with this and several other members of the TRAF family, which may be essential for the oncogenic effects of LMP1. Several alternatively spliced transcript variants encoding three distinct isoforms have been reported.
CD40 associated protein 1
, CD40 binding protein
, CD40 receptor associated factor 1
, LMP1-associated protein 1
, CD40 receptor-associated factor 1
, TNF receptor-associated factor 3