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

Fadd Antibodies for Homo sapiens (Human)

Fadd Antibodies for Mus musculus (Mouse)

Fadd Antibodies for Drosophila melanogaster (Fruit fly)

Fadd Antibodies for Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

Fadd Antibodies for Escherichia coli (strain K12)

Fadd Antibodies for Escherichia coli O157:H7

Fadd Proteins

Fadd Proteins for Escherichia coli (strain K12)

Fadd Proteins for Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

Fadd Proteins for Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Fadd Proteins for Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

Fadd Proteins for Salmonella typhi

Fadd Proteins for Homo sapiens (Human)

Fadd Proteins for Drosophila pseudoobscura pseudoobscura (Fruit fly)

Fadd Proteins for Mus musculus (Mouse)

Fadd Proteins for Bos taurus (Bovine)

Fadd Proteins for Escherichia coli O157:H7

Fadd Proteins for Yersinia pestis

Fadd Proteins for Drosophila melanogaster (Fruit fly)

Fadd ELISA Kit

Fadd ELISA Kit for Homo sapiens (Human)

Fadd Background

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.

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1