FAS-associated death domain protein is a protein in humans that is encoded by FADD gene. Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling.
The following FADD reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.
FADD Antibodies for Homo sapiens (Human)
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA007958GA01HU | FADD Antibody |
Human,Mouse,Rat | ELISA,WB,IHC |
CSB-PA623788ESR1HU | FADD Antibody |
Human | ELISA, IHC |
CSB-PA446731 | Phospho-FADD (Ser191) Antibody |
Human,Mouse | ELISA,WB,IHC |
CSB-PA002463 | FADD Antibody |
Human | WB, IHC, ELISA |
CSB-PA070144 | Phospho-FADD (S194) Antibody |
Human | WB, IHC, ELISA |
CSB-PA070145 | FADD Antibody |
Human | IHC, IF, ELISA |
CSB-PA824751 | FADD Antibody |
Human,Mouse | ELISA,WB,IHC |
CSB-PA221364 | FADD Antibody |
Human | ELISA,IHC |
FADD Antibodies for Mus musculus (Mouse)
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA975869 | FADD (Ab-191) Antibody |
Human,Mouse | ELISA,WB |
CSB-PA006346 | Phospho-FADD (S191) Antibody |
Mouse | WB, IHC, ELISA |
CSB-PA011057 | FADD Antibody |
Mouse | WB, IHC, ELISA |
FADD Antibodies for Drosophila melanogaster (Fruit fly)
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA893221XA01DLU | Fadd Antibody |
Drosophila melanogaster (Fruit fly) | ELISA, WB (ensure identification of antigen) |
FADD Antibodies for Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA302467XA01FQR | fadD Antibody |
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) | ELISA, WB (ensure identification of antigen) |
FADD Antibodies for Escherichia coli (strain K12)
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA300208XA01ENV | fadD Antibody |
Escherichia coli (strain K12) | ELISA, WB (ensure identification of antigen) |
CSB-PA300208ZA01ENV | fadD Antibody |
Escherichia coli | ELISA, WB (ensure identification of antigen) |
FADD Antibodies for Escherichia coli O157:H7
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA834851XA01EOD | fadD Antibody |
Escherichia coli O157:H7 | ELISA, WB (ensure identification of antigen) |
FADD Proteins for Escherichia coli (strain K12)
Code | Product Name | Source |
---|---|---|
CSB-YP300208ENV CSB-BP300208ENV CSB-MP300208ENV CSB-EP300208ENV-B |
Recombinant Escherichia coli Long-chain-fatty-acid--CoA ligase (fadD) |
Yeast Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
CSB-EP300208ENV | Recombinant Escherichia coli Long-chain-fatty-acid--CoA ligase (fadD) |
E.coli |
FADD Proteins for Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Code | Product Name | Source |
---|---|---|
CSB-YP302467EGX CSB-EP302467EGX CSB-BP302467EGX CSB-MP302467EGX CSB-EP302467EGX-B |
Recombinant Long-chain-fatty-acid--CoA ligase (fadD) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
FADD Proteins for Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Code | Product Name | Source |
---|---|---|
CSB-YP342804HTA CSB-EP342804HTA CSB-BP342804HTA CSB-MP342804HTA CSB-EP342804HTA-B |
Recombinant Haemophilus influenzae Long-chain-fatty-acid--CoA ligase (fadD), partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
FADD Proteins for Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Code | Product Name | Source |
---|---|---|
CSB-YP351269SXB CSB-EP351269SXB CSB-BP351269SXB CSB-MP351269SXB CSB-EP351269SXB-B |
Recombinant Salmonella typhimurium Long-chain-fatty-acid--CoA ligase (fadD), partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
FADD Proteins for Salmonella typhi
Code | Product Name | Source |
---|---|---|
CSB-YP351875SWW CSB-EP351875SWW CSB-BP351875SWW CSB-MP351875SWW CSB-EP351875SWW-B |
Recombinant Long-chain-fatty-acid--CoA ligase (fadD), partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
FADD Proteins for Homo sapiens (Human)
Code | Product Name | Source |
---|---|---|
CSB-YP623788HU CSB-BP623788HU CSB-MP623788HU CSB-EP623788HU-B |
Recombinant Human FAS-associated death domain protein (FADD) |
Yeast Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
FADD Proteins for Drosophila pseudoobscura pseudoobscura (Fruit fly)
Code | Product Name | Source |
---|---|---|
CSB-YP639067DME CSB-EP639067DME CSB-BP639067DME CSB-MP639067DME CSB-EP639067DME-B |
Recombinant Drosophila pseudoobscura pseudoobscura Death domain-containing adapter protein BG4 (BG4) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
FADD Proteins for Mus musculus (Mouse)
Code | Product Name | Source |
---|---|---|
CSB-YP730727MO CSB-EP730727MO CSB-BP730727MO CSB-MP730727MO CSB-EP730727MO-B |
Recombinant Mouse Protein FADD (Fadd) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
FADD Proteins for Bos taurus (Bovine)
Code | Product Name | Source |
---|---|---|
CSB-YP737367BO CSB-EP737367BO CSB-BP737367BO CSB-MP737367BO CSB-EP737367BO-B |
Recombinant Bovine Protein FADD (FADD) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
FADD Proteins for Escherichia coli O157:H7
Code | Product Name | Source |
---|---|---|
CSB-YP834851EOD CSB-EP834851EOD CSB-BP834851EOD CSB-MP834851EOD CSB-EP834851EOD-B |
Recombinant Escherichia coli O157:H7 Long-chain-fatty-acid--CoA ligase (fadD) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
FADD Proteins for Yersinia pestis
Code | Product Name | Source |
---|---|---|
CSB-YP835296YAS CSB-EP835296YAS CSB-BP835296YAS CSB-MP835296YAS CSB-EP835296YAS-B |
Recombinant Long-chain-fatty-acid--CoA ligase (fadD), partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
FADD Proteins for Drosophila melanogaster (Fruit fly)
Code | Product Name | Source |
---|---|---|
CSB-YP893221DLU CSB-EP893221DLU CSB-BP893221DLU CSB-MP893221DLU CSB-EP893221DLU-B |
Recombinant Drosophila melanogaster Death domain-containing adapter protein BG4 (BG4) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
FADD ELISA Kit for Homo sapiens (Human)
Code | Product Name | Sample Types | Sensitivity |
---|---|---|---|
CSB-EL007958HU | Human Protein FADD(FADD) ELISA kit |
serum, plasma, cell culture supernates, cell lysates | 31.25 pg/mL |
FAS-associated death domain protein (FADD), also known as MORT1, is an adapter protein essential for the induction of extrinsic apoptosis. FADD contains a C-terminal death domain (DD) and an N-terminal death effector domain (DED) [1]. During extrinsic apoptosis, FADD acts as a bridge between the ligated death receptor and the caspases that directly propagate apoptotic signals. The receptors of the tumor necrosis factor (TNF) superfamily such as the FAS receptor, interacts with its cognate ligand to form a trimer complex. FADD binds to the FAs receptor trimer through its DD [2][3]. FADD is activated and subsequently recruits apoptotic pro-caspases via DED/DED interactions to form the death-inducing signal complex (DISC), which allows cleavage and activation of initiator caspases-8 and caspases-10, ultimately leading to the apoptotic response [4]. FADD is also involved in initiating necroptosis with serine/threonine kinases RIPK1 and RIPK3 [5]. Apart from being an essential component in death receptor-mediated apoptosis, FADD is required for T-cell proliferation, cell cycle progression, tumor development, inflammation, innate immunity, and autophagy [6]. It has been confirmed that apoptosis is dysregulated in various pathological conditions. In cancer, loss of FADD is beneficial to the survival of malignant tumor cells by preventing apoptosis. Elevated FADD expression has been detected in human lung cancer and is correlated with poor survival [7]. FADD expression is increased in white blood cells of multiple sclerosis relapsing patients, suggesting that FADD functions in the underlying inflammatory processes [8]. And overexpression of FADD and caspase-8 may play a role in TNF-mediated apoptosis of dopaminergic neurons of patients with Parkinson's disease [9]. In terms of FADD's role in numerous cell death processes, it is promising to be a therapeutic target in many conditions such as malignancy, autoimmunity, and inflammation. Marín-Rubio JL et al.proposed that FADD expression and phosphorylation may be reliable biomarkers with prognostic value for T-cell lymphoblastic lymphoma (T-LBL) stratification [10].
[1] Carrington PE, Sandu C, et al. The structure of FADD and its mode of interaction with procaspase-8 [J]. Mol Cell. 2006 Jun 9;22(5):599-610.
[2] Boldin, M. P., Varfolomeev, E. E., et al. A Novel Protein That Interacts with the Death Domain of Fas/APO1 Contains a Sequence Motif Related to the Death Domain [J]. Journal of Biological Chemistry. 1995, 270 (14): 7795–7798.
[3] Chinnaiyan, A. M., K. O’Rourke, M. Tewari, et al. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis [J]. Cell 1995, 81: 505-512.
[4] Eberstadt, M., B. Huang, Z. Chen, et al. NMR structure and mutagenesis of the FADD (Mort1) death-effector domain [J]. Nature 1998, 392: 941-945.
[5] Lee EW, Seo J, et al. The roles of FADD in extrinsic apoptosis and necroptosis [J]. BMB Rep. 2012 Sep;45(9):496-508.
[6] Tourneur L, Chiocchia G. FADD: a regulator of life and death [J]. Trends Immunol 2010; 31:260-9.
[7] Chen G, Bhojani MS, et al. Phosphorylated FADD induces NF-kappaB, perturbs cell cycle, and is associated with poor outcome in lung adenocarcinomas [J]. Proc Natl Acad Sci U S A 2005; 102:12507-12.
[8] Reinhard Reuss, Marta Mistarz, et al. FADD is upregulated in relapsing remitting multiple sclerosis [J]. Neuroimmunomodulation, 01 Mar 2014, 21(5):221-225.
[9] Hartmann A, Mouatt-Prigent A, et al. FADD: A link between TNF family receptors and caspases in Parkinson's disease [J]. Neurology, 01 Jan 2002, 58(2):308-310.
[10] Marín-Rubio JL, de Arriba MC, et al. Deregulated FADD expression and phosphorylation in T-cell lymphoblastic lymphoma [J]. Oncotarget. 2016 Sep 20;7(38):61485-61499.