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anti-Human FADD Antikörper:
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Human Polyclonal FADD Primary Antibody für WB - ABIN1881331
Papoff, Trivieri, Crielesi, Ruberti, Marsilio, Ruberti: FADD-calmodulin interaction: a novel player in cell cycle regulation. in Biochimica et biophysica acta 2010
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Human Polyclonal FADD Primary Antibody für IP, WB - ABIN549241
Piazzolla, Meissl, Kucerova, Rubiolo, Baccarini: Raf-1 sets the threshold of Fas sensitivity by modulating Rok-alpha signaling. in The Journal of cell biology 2005
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Monoclonal FADD Primary Antibody für ELISA, WB - ABIN533782
Bannerman, Tupper, Kelly, Winn, Harlan: The Fas-associated death domain protein suppresses activation of NF-kappa B by LPS and IL-1 beta. in The Journal of clinical investigation 2002
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Human Polyclonal FADD Primary Antibody für IP, WB - ABIN222894
Chen, Texada, Duggan, Liang, Reden, Kooragayala, Langford: Surface calreticulin mediates muramyl dipeptide-induced apoptosis in RK13 cells. in The Journal of biological chemistry 2005
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Human Polyclonal FADD Primary Antibody für IHC, WB - ABIN6711963
Hu, Xu, Yin, Qi, Li, Xu, Han, Peng, Wan: Cytotoxicity of dioscin in human gastric carcinoma cells through death receptor and mitochondrial pathways. in Journal of applied toxicology : JAT 2014
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Human Polyclonal FADD Primary Antibody für IHC (p), WB - ABIN669471
Soni, Adebiyi: Early septic insult in neonatal pigs increases serum and urinary soluble Fas ligand and decreases kidney function without inducing significant renal apoptosis. in Renal failure 2016
Human Polyclonal FADD Primary Antibody für IHC, WB - ABIN2792110
Thomas, Henson, Reed, Salsbury, Thorburn: Direct binding of Fas-associated death domain (FADD) to the tumor necrosis factor-related apoptosis-inducing ligand receptor DR5 is regulated by the death effector domain of FADD. in The Journal of biological chemistry 2004
Human Polyclonal FADD Primary Antibody für IHC, WB - ABIN6680042
Tian, Yao, Yang, Ren, Jiao, Zhang, Li, Zhang, Xia, Qin: D4F alleviates macrophage-derived foam cell apoptosis by inhibiting the NF-κB-dependent Fas/FasL pathway. in Scientific reports 2017
K6-linked ubiquitylation of FADD by CHIP is a crucial checkpoint in cytokine-dependent extrinsic apoptosis.
Overexpression of FADD and Caspase-8 suppresses proliferation whilst promoting the apoptosis of human GBM cells.
FADD expression and its phosphorylation can be reliable biomarkers with prognostic value for T-cell lymphoblastic lymphoma stratification.
FADD interference down-regulated Rheb expression and repressed mTORC1 activity in breast cancer cell lines. The autophagy was induced by FADD deficiency in MCF7 or MDA-231 cells but rescued by recovering Rheb expression.
The present data suggests FADD as a putative biomarker for pathological processes associated with the course of clinical dementia.
at normal levels of expression during bacterial infection, NleB1/NleB(CR) antagonizes death receptor-induced apoptosis of infected cells by modifying FADD in an irreversible manner.
Caspase-8 can serve in two distinct roles in response to TRAIL receptor engagement, as a scaffold for assembly of a Caspase-8-FADD-RIPK1 "FADDosome" complex, leading to NFkappaB-dependent inflammation, or as a protease that promotes apoptosis.
Using the tDED filament structure as a template, structural analyses reveal the interaction surfaces between FADD and caspase-8 and the distinct mechanisms of regulation by cFLIP and MC159 through comingling and capping, respectively.
This study reveals an essential role of SUMOylated FADD in Drp1- and caspase-10-dependent necrosis.
In myelodysplastic syndrome, FADD expression is regulated by SPAG6 which influences its interaction with TRAIL death receptors.
High levels of FADD and caspase-8, but not caspase-3, were associated with increased incidence of coronary events in subjects from the general population.
Both Fas associated via death domain gene copy number amplification and high protein expression were significantly associated with lymph node metastasis and had the shortest disease-free survival and overall survival.
FADD, as well as NEMO, is a substrate for LUBAC ubiquitin ligase (E3) complex, composed of the HOIP, HOIL-1L, and SHARPIN subunits.
autoinflammation-associated H443P nlrc4 mutant is altered in interaction with SUG1 and ubiquitinated proteins, triggering constitutive caspase-8-mediated cell death dependent on FADD but independent of Ser(533) phosphorylation.
this study shows that C5a signaling induces apoptosis in brain vascular endothelial cells in experimental lupus through activation of FADD
Authors identify non-canonical nuclear factor-kappaB (NF-kappaB) signaling up regulated and it was directly linked with the tumor necrosis with MT2A and pFADD genes. pFADD with MT2A can inhibit the apoptosis and promote proliferation, of colorectal cancer cells.
knockdown of cFLIPL and induced expression of FADD rapidly accumulate intracellular ROS accompanied by JNK1 activation to substantiate apoptosis.
Data indicate that FADD mediated apoptotic cell death was directed by ubiquitination of cFLIPL and inhibition of NF-kappaB activation.
Structural analysis for the roles of DR5 death domain mutations on oligomerization of DR5 death domain-FADD complex in the death-inducing signaling complex formation has been presented.
A20 targets caspase-8 and FADD to protect HTLV-I-infected cells.
results show that N-FADD is a more potent apoptotic inducer and VNP20009-mediated targeted expression of N-FADD provides a possible cancer gene therapeutic approach for the treatment of melanoma.
these results demonstrated that RIPK3-mediated signaling in Tie-2 expressing cells was responsible for the embryonic lethality of Fadd-/- with cardiac failure.
The study provides genetic evidence that different RIP1 kinase inactive mutations have distinct impacts on the embryogenesis of Fadd-deficient mice.
Our findings reveal that MLKL and FADD play critical roles in preventing lymphoproliferative disease and activating the NLRP3 inflammasome
miR-7a was a necessary mediator in FADD-regulated FAK expression. In contrast to its classical apoptotic role, FADD interference could reduce the rate of cell migration, which could be rescued by inhibiting miR-7a expression.
In macrophages, ultraviolet radiation induced association of MyD88 with FADD and migration of FADD to the cell membrane
The authors conclude that FADD is a master regulator of glucose and fat metabolism.
Mice deficient in RIPK3 or doubly deficient in MLKL and FADD, but not MLKL alone, are more susceptible to influenza A virus than their wild-type counterparts, revealing an important role for RIPK3-mediated apoptosis in antiviral immunity.
Wild-type cells can execute apoptosis via both, the mitochondrial and the receptor-mediated pathway whereas FADD-deficient cells can only activate the intrinsic pathway. There is a difference in UVC radiation response between two cell lines indicating the role of FADD in the selection of cell death modality.
Deletion of FADD in macrophages and granulocytes results in RIP3- and MyD88-dependent systemic inflammation.
A constitutively phosphoryl-mimicking mutation of Fas-associated death domain (FADD-D) enhances Notch-1 signaling and compromises Wnt signaling in both cultured myoblasts and regenerating muscles.
Beta amyloid-induced upregulation of death receptor 6 accelerates the toxic effect of N-terminal fragment of amyloid precursor protein
Phosphorylation of FADD by the kinase CK1alpha promotes KRASG12D-induced lung cancer.
This study evaluated the role of FADD in pancreatic islets and insulin secretion.
depletion of alphaNAC in multiple types of cancer cells induce typical apoptotic cell death. This anti-apoptotic function is mediated by the FADD/c-Jun N-terminal kinase pathway.
These data suggest that as a death receptor, FADD is also required for cell survival in beta-selection as a regulator of Notch1 expression.
using T-cell specific deletion mice, we observed that FADD deficiency in thymocytes led to increased apoptosis and reduced cell numbers, which may be attributed to the reduction of Glut1 expression and correspondingly decreased glucose uptake
FADD induces apoptosis
mapping and sequencing of bovine FADD cDNA, and characterization of its expression in endothelial cells
FADD has multiple functions in embryos; it plays a part in the regulation of NF-kappaB activation and heart formation, in addition to apoptosis.
The FADD protein shows evolutionary conservation.
Interaction of xFADD and xRIP1 induced synergistic activation of JNK and NF-kappaB.
establish that pax2 in combination with vax2 directly regulate the fas-associated death domain (fadd) gene
The protein encoded by this gene is an adaptor molecule that interacts with various cell surface receptors and mediates cell apoptotic signals. Through its C-terminal death domain, this protein can be recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and thus it participates in the death signaling initiated by these receptors. Interaction of this protein with the receptors unmasks the N-terminal effector domain of this protein, which allows it to recruit caspase-8, and thereby activate the cysteine protease cascade. Knockout studies in mice also suggest the importance of this protein in early T cell development.
Fas-associating death domain-containing protein
, Fas-associating protein with death domain
, growth-inhibiting gene 3 protein
, mediator of receptor induced toxicity
, mediator of receptor-induced toxicity
, protein FADD
, FAS-associated death domain protein
, FAS-associating death domain-containing protein
, Fas (TNF receptor superfamily, member 6)
, Fas-associated via death domain
, Fas (TNFRSF6)-associated via death domain
, Fas associated via death domain S homeolog