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anti-Human TRAF3 Antikörper:
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Human Polyclonal TRAF3 Primary Antibody für WB - ABIN6713228
Yu, Deng, Lu, Jia, Wu, Qi: Systemic cytokine profiles and splenic toll-like receptor expression during Trichinella spiralis infection. in Experimental parasitology 2013
Human Polyclonal TRAF3 Primary Antibody für IHC, IHC (p) - ABIN4361674
Zapata, Krajewska, Krajewski, Kitada, Welsh, Monks, McCloskey, Gordon, Kipps, Gascoyne, Shabaik, Reed: TNFR-associated factor family protein expression in normal tissues and lymphoid malignancies. in Journal of immunology (Baltimore, Md. : 1950) 2000
Human Polyclonal TRAF3 Primary Antibody für IHC (p), WB - ABIN4361672
Agrawal, Rastogi, Dogra, Pandey, Basu, Singh: Chandipura virus changes cellular miRNome in human microglial cells. in Journal of medical virology 2019
Human Polyclonal TRAF3 Primary Antibody für ELISA, WB - ABIN1003295
Arch, Gedrich, Thompson: Tumor necrosis factor receptor-associated factors (TRAFs)--a family of adapter proteins that regulates life and death. in Genes & development 1998
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Human Polyclonal TRAF3 Primary Antibody für ICC, ELISA - ABIN1003296
van Eyndhoven, Gamper, Cho, Mackus, Lederman: TRAF-3 mRNA splice-deletion variants encode isoforms that induce NF-kappaB activation. in Molecular immunology 1999
Show all 4 Pubmed References
Results found that TRAF3IP3 mediates TRAF3 recruitment to MAVS upon virus infection.
Study results indicate that TRAF3, perhaps by promoting exacerbated B cell responses to certain antigens, and BCL2, presumably by supporting survival of these clones, cooperate to induce mature B cell neoplasms in transgenic mice expressing human proteins. TRAF3 upregulation favors the production of V(H)DJ(H) rearrangements producing HCDR3 sequences similar to those recognizing PAMPs and DAMPs.
TRAF3 protein levels decrease in bone and bone marrow during aging in mice and humans. Development of drugs to prevent TRAF3 degradation in immune and bone cells could be a novel therapeutic approach to prevent or reduce bone loss and the incidence of several common diseases associated with aging.
Overexpression of TRAF3 in HPV(+) cell lines with decreased endogenous TRAF3 inhibited NF-kappaB2/RELB expression, nuclear localization, and NF-kappaB reporter activity, while increasing the expression of IFNA1 mRNA and protein and sensitizing cells to its growth inhibition. Overexpression of TRAF3 also enhanced TP53 and RB tumor suppressor proteins and decreased HPV E6 oncoprotein in HPV(+) cells
TRAF3 is also now known to function as a resident nuclear protein, and to impact B cell metabolism. Through these and additional mechanisms TRAF3 exerts powerful restraint upon B cell survival and activation. It is thus perhaps not surprising that TRAF3 has been revealed as an important tumor suppressor in B cells.
The present study confirms that genes involved in activation of NF-kappaB-signaling pathways are a major driver in oncogenesis of H. pylori eradication-resistant gastric marginal zone lymphoma and revealed that TRAF3 mutation is a major contributor in MALT1 rearrangement-negative gastric marginal zone lymphoma.
The authors found that tumor necrosis factor receptor-associated factor 2 (TRAF2), as well as TRAF1 and 3, directly binds to the active caspase-2 dimer.
The findings suggest that Parkin plays a novel role in innate immune signaling by targeting TRAF3 for degradation and maintaining the balance of innate antiviral immunity.
Study identified that TRAF3 was a direct and functional target of the miR-17-92 cluster in MGC-803 gastric cancer cells. The loss-of-function of TRAF3 led to the acquirement of phenotypes, like what had been observed in the MGC-803 cells overexpressing the miR-17-92 cluster. Survival analyses revealed that TRAF3 served as an important prognostic indicator in patients with gastric cancer.
A TRAF3-NIK axis differentially regulates viral DNA vs RNA pathways in innate immune signaling.
Association between the rs1883832 and rs3765459 CD40 gene polymorphism and susceptibility to cervical cancer in a subset of Malaysian population.
Study demonstrated that TRAF3, as a novel RIP2 binding partner, was downregulated in glioma tissues and functionally was a negative regulator involved in RIP2induced glioma cell growth.
Data show that TNF receptor-associated factor 3 (TRAF3) autophagy is driven by RAS and results in activation of transcription factor RelB (RELB).
MicroRNA-214 regulates immunity-related genes in bovine mammary epithelial cells by targeting NFATc3 and TRA
These results indicate that TRAF3 deficiency suffices to metabolically reprogram B cells, a finding that improves our understanding of the role of TRAF3 as a tumor suppressor, and suggests potential therapeutic strategies.
Viral proteins aim to subvert TRAF3 antiviral action.
Mechanistic studies showed that HACE1 exerts its inhibitory role on virus-induced signaling by disrupting the MAVS-TRAF3 complex.
An important B cell-specific role for TNFR-associated factor 3 is the inhibition of homeostatic survival, directly relevant to the common occurrence of TNFR-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 receptor-associated factor 3) and CYLD (cylindromatosis lysine 63 deubiquitinase). Defects in TRAF3 and CYLD 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
these results suggest that JNK1-mediated autophagy could promote RANKL-induced osteoclastogenesis via enhancing TRAF3 degradation. Importantly, JNK1 could prevent OCP apoptosis through autophagy-TRAF3 signaling, which provides more potential targets for clinical treatment of pathological bone loss.
The finding that mice with TRAF3 deleted in mesenchymal precursors have increased bone resorption and decreased bone formation, points to TRAF3 having a positive regulatory role in osteoblastic precursors that could be targeted therapeutically to not only inhibit bone resorption, but also stimulate bone formation in common diseases associated with decreased bone mass.
In the absence of HECTD3, type I IFN response was impaired during bacterial infection both in vivo and in vitro. HECTD3 regulated type I IFN production by mediating K63-linked polyubiquitination of TRAF3 at residue K138. The catalytic domain of HECTD3 regulated TRAF3 K63 polyubiquitination, which enabled TRAF3-TBK1 complex formation.
IL-17A modulates apoptosis of osteoclast precursors through Beclin1-autophagy-TRAF3 signaling pathway, thereby influencing osteoclastogenesis.
TRAF3 positively regulates mesenchymal progenitor cells (MPC) differentiation into osteoblasts. TRAF3 deletion in MPCs activated NF-kappaB RelA and RelB to promote RANKL expression and enhance bone destruction.
TRAF2 is essential but TRAF3 is dispensable for T cell-dependent humoral immunity and CD40-induced class switch recombination
TRAF3 plays a negative role in platelet activation and in thrombus formation in vivo.
TRAF3 knockdown-reduced apoptosis, inflammatory response and oxidative stress were significantly rescued by promoting JNK activity in LPS and H2O2-cotreated cardiomyocytes.
The overexpression of TRAF3 attenuated the proinflammatory effects of USP25 knockdown in tolerized Kupffer cells.
Rela and Traf3 were both targeted by miR-155-5p.
TRAF3 promotes T cell activation by regulating localization and functions of Csk and PTPN22.
osteoclast-targeted antagomir-214-3p delivery could recover the TRAF3 protein expression and attenuate the development of osteolytic bone metastasis.
Depletion of LAP1 during early embryonic myogenesis leads to growth retardation and premature death.
In B lymphocytes, TNFR-associated factor 3 inhibits signaling by TNFR superfamily receptors, Toll-like receptors, and interleukin-6R. In T lymphocytes, TNFR-associated factor 3 is required for normal signaling by the T cell antigen receptor, while inhibiting signaling by the interleukin-2 receptor. Cytoplasmic TNFR -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 signaling pathway Bcl-2 and Bcl-xl 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 enhances TNF-induced osteoclast formation from precursor spleen cells and enhances bone resorption independently of Traf6 by degrading Traf3, a known inhibitor of osteoclastogenesis. (RANKL = osteoclast differentiation factor; TNF = tumor necrosis factor; Traf = TNF receptor-associated factor)
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