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anti-Human FADD Antibodies:
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Human Monoclonal FADD Primary Antibody for IF, IP - ABIN967945
Chang, Xing, Pan, Algeciras-Schimnich, Barnhart, Yaish-Ohad, Peter, Yang: c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis. in The EMBO journal 2002
Show all 5 Pubmed References
Human Polyclonal FADD Primary Antibody for 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 Monoclonal FADD Primary Antibody for IF, IP - ABIN967944
MacFarlane, Harper, Snowden, Dyer, Barnett, Pringle, Cohen: Mechanisms of resistance to TRAIL-induced apoptosis in primary B cell chronic lymphocytic leukaemia. in Oncogene 2002
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Human Monoclonal FADD Primary Antibody for WB - ABIN967598
Alappat, Volkland, Peter: Cell cycle effects by C-FADD depend on its C-terminal phosphorylation site. in The Journal of biological chemistry 2003
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Human Polyclonal FADD Primary Antibody for 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
Show all 3 Pubmed References
Human Monoclonal FADD Primary Antibody for IP, WB - ABIN967524
Cleveland, Ihle: Contenders in FasL/TNF death signaling. in Cell 1995
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Human Polyclonal FADD Primary Antibody for 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 for 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
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 (show CASP8 Antibodies) and the distinct mechanisms of regulation by cFLIP (show CFLAR Antibodies) and MC159 through comingling and capping, respectively.
This study reveals an essential role of SUMOylated FADD in Drp1 (show CRMP1 Antibodies)- and caspase-10 (show CASP10 Antibodies)-dependent necrosis.
In myelodysplastic syndrome, FADD expression is regulated by SPAG6 (show SPAG6 Antibodies) which influences its interaction with TRAIL death receptors.
High levels of FADD and caspase-8 (show CASP8 Antibodies), but not caspase-3 (show CASP3 Antibodies), 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 (show IKBKG Antibodies), is a substrate for LUBAC ubiquitin ligase (E3) complex, composed of the HOIP (show RNF31 Antibodies), HOIL-1L (show RBCK1 Antibodies), and SHARPIN (show SHARPIN Antibodies) subunits.
autoinflammation-associated H443P nlrc4 (show NLRC4 Antibodies) mutant is altered in interaction with SUG1 (show PSMC5 Antibodies) and ubiquitinated proteins, triggering constitutive caspase-8 (show CASP8 Antibodies)-mediated cell death dependent on FADD but independent of Ser (show SIGLEC1 Antibodies)(533) phosphorylation.
The authors conclude that FADD is a master regulator of glucose and fat metabolism.
Mice deficient in RIPK3 (show RIPK3 Antibodies) 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 (show RIPK3 Antibodies)-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.
knockdown of cFLIPL and induced expression of FADD rapidly accumulate intracellular ROS (show ROS1 Antibodies) accompanied by JNK1 (show MAPK8 Antibodies) activation to substantiate apoptosis.
A20 targets caspase-8 and FADD to protect HTLV-I-infected cells.
Deletion of FADD in macrophages and granulocytes results in RIP3 (show MPRIP Antibodies)- and MyD88 (show MYD88 Antibodies)-dependent systemic inflammation.
A constitutively phosphoryl-mimicking mutation of Fas (show FAS Antibodies)-associated death domain (FADD-D) enhances Notch-1 (show NOTCH1 Antibodies) signaling and compromises Wnt (show WNT2 Antibodies) signaling in both cultured myoblasts and regenerating muscles.
Beta amyloid-induced upregulation of death receptor 6 (show TNFRSF21 Antibodies) accelerates the toxic effect of N-terminal fragment of amyloid precursor protein (show APP Antibodies)
Phosphorylation of FADD by the kinase CK1alpha (show CSNK1A1 Antibodies) promotes KRASG12D-induced lung cancer.
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 (show NFKB1 Antibodies) activation and heart formation, in addition to apoptosis.
The FADD protein shows evolutionary conservation.
Interaction of xFADD and xRIP1 induced synergistic activation of JNK (show MAPK8 Antibodies) and NF-kappaB (show NFKB1 Antibodies).
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