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FADD monoclonal antibody (1F7)

ADI-AAM-212-E 100 µg 393.00 USD
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Product Details

Alternative Name:MORT1, Fas (TNFRSF6)-associated via death domain
Immunogen:Recombinant human FADD.
UniProt ID:Q13158
Species reactivity:Human, Mouse
Recommended Dilutions/Conditions:Western Blot (1µg/ml, ECL)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
Application Notes:Detects a band of ~28kDa by Western blot.
Purity Detail:Protein A affinity purified.
Formulation:Liquid. In PBS, pH 7.2, with 50% glycerol.
Shipping:Blue Ice
Long Term Storage:-20°C
Scientific Background:Fas-associating death domain containing protein (FADD)/MORT1 serves as a signal transducer of Fas-induced apoptosis. Through its amino-terminal death effector domain (DED), FADD binds to cytosolic proteins such as TRADD, a cytosolic death domaincontaining protein that asssociates with the cytosolic portion of TNF receptor, or MACH/FLICE/caspase-8, a protease with sequence homology to ICE-CED-3 protease family, in order to transduce the death signal.
Regulatory Status:RUO - Research Use Only
FADD monoclonal antibody (1F7) Western blot
Western blot probed with FADD mAb (1F7). Lane 1 FADD (recombinant) and cell lysates Jurkat (lane 2), Raji (lane 3), HeLa (lane 4), ZR75-1 (lane 5), A431 (lane 6), and HUC-Fm (lane 7).
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FADD monoclonal antibody (1F7) Western blot

Product Literature References

Bioluminescent RIPoptosome Assay for FADD/RIPK1 Interaction Based on Split Luciferase Assay in a Human Neuroblastoma Cell Line SH-SY5Y: P. Ghanavatian, et al.; Biosensors 13, 297 (2023), Abstract;
Upregulation of RIPK1 implicates in HEK 293T cell death upon transient transfection of A53T-α-synuclein: F. Meshkini, et al.; Int. J. Biol. Macromol. 230, 123216 (2023), Abstract;
Tankyrase-mediated ADP-ribosylation is a regulator of TNF-induced death: L. Liu, et al.; Sci. Adv. 8, eabh2332 (2022), Abstract;
Antioxidant and food additive BHA prevents TNF cytotoxicity by acting as a direct RIPK1 inhibitor: T. Delanghe, et al.; Cell Death Dis. 12, 699 (2021), Abstract;
RIPK1 dephosphorylation and kinase activation by PPP1R3G/PP1γ promote apoptosis and necroptosis: J. Du, et al.; Nat. Commun. 12, 7067 (2021), Abstract;
Autophosphorylation at serine 166 regulates RIP kinase 1-mediated cell death and inflammation: L. Laurien, et al.; Nat. Commun. 11, 1747 (2020), Abstract; Full Text
Tristetraprolin regulates necroptosis during tonic Toll-like receptor 4 (TLR4) signaling in murine macrophages: A. Ariana, et al.; J. Biol. Chem. 295, 4661 (2020), Abstract; Full Text
Serine 25 phosphorylation inhibits RIPK1 kinase-dependent cell death in models of infection and inflammation: Y. Dondelinger, et al.; Nat. Commun. 10, 1729 (2019), Abstract; Full Text
N-glycosylation of mouse TRAIL-R restrains TRAIL-induced apoptosis: Y. Estornes, et al.; Cell Death Dis. 9, 494 (2018), Abstract; Full Text
MK2 phosphorylation of RIPK1 regulates TNF-mediated cell death: Y. Dondelinger, et al.; Nat. Cell Biol. 19, 1237 (2017), Abstract;
The linear ubiquitin chain assembly complex regulates TRAIL-induced gene activation and cell death: E. Lafont, et al.; EMBO J. 36, 1147 (2017), Abstract; Full Text
When PERK inhibitors turn out to be new potent RIPK1 inhibitors: critical issues on the specificity and use of GSK2606414 and GSK2656157: D. Rojas-Rivera, et al.; Cell Death Differ. 24, 1100 (2017), Abstract; Full Text
SPATA2 promotes CYLD activity and regulates TNF-induced NF-κB signaling and cell death: L. Schlicher, et al.; EMBO Rep. 17, 1485 (2016), Abstract; Full Text
γ-Secretase Activity Is Required for Regulated Intramembrane Proteolysis of Tumor Necrosis Factor (TNF) Receptor 1 and TNF-mediated Pro-apoptotic Signaling: J. Chhibber-Goel, et al.; J. Biol. Chem. 291, 5971 (2016), Abstract; Full Text
CYLD and the NEMO Zinc Finger Regulate Tumor Necrosis Factor Signaling and Early Embryogenesis: Y. Zhao, et al.; J. Biol. Chem. 90, 22076 (2015), Application(s): Western Blot, Abstract;
In mouse embryonic fibroblasts, neither caspase-8 nor cellular FLICE-inhibitory protein (FLIP) is necessary for TNF to activate NF-κB, but caspase-8 is required for TNF to cause cell death, and induction of FLIP by NF-κB is required to prevent it: D.M. Moujalled, et al.; Cell Death Dis. 19, 808 (2012), Abstract; Full Text

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