≡

Fas Associating Death Domain Containing Protein (FADD)

[Edit]

GIG3; MORT1; FADD Death Effector Domain; Fas-Associated Protein With Death Domain; Mediator Of Receptor-Induced Toxicity; Growth-Inhibiting Gene 3

Fas Associating Death Domain Containing Protein (FADD)
CCC K078
HGNC 3573
MGI 109324
PubMed 15549108
RGD 628700
UniProt Q13158
Wiki FADD
FADD is an adaptor molecule that bridges the Fas-receptor, and other death receptors, to caspase-8 through its death domain to form the death inducing signaling complex during apoptosis. 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.

Organism species: Homo sapiens (Human)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPK078Hu01 Recombinant Fas Associating Death Domain Containing Protein (FADD) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAK078Hu01 Polyclonal Antibody to Fas Associating Death Domain Containing Protein (FADD) WB; IHC; ICC; IP.
Assay Kits SEK078Hu ELISA Kit for Fas Associating Death Domain Containing Protein (FADD) Enzyme-linked immunosorbent assay for Antigen Detection.

Organism species: Mus musculus (Mouse)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPK078Mu01 Recombinant Fas Associating Death Domain Containing Protein (FADD) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAK078Mu01 Polyclonal Antibody to Fas Associating Death Domain Containing Protein (FADD) WB,IHC
Assay Kits n/a CLIA Kit for Fas Associating Death Domain Containing Protein (FADD) CLIA Kit Customized Service Offer
n/a ELISA Kit for Fas Associating Death Domain Containing Protein (FADD) ELISA Kit Customized Service Offer

Organism species: Rattus norvegicus (Rat)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins n/a Recombinant Fas Associating Death Domain Containing Protein (FADD) Recombinant Protein Customized Service Offer
Antibodies n/a Monoclonal Antibody to Fas Associating Death Domain Containing Protein (FADD) Monoclonal Antibody Customized Service Offer
n/a Polyclonal Antibody to Fas Associating Death Domain Containing Protein (FADD) Polyclonal Antibody Customized Service Offer
Assay Kits n/a CLIA Kit for Fas Associating Death Domain Containing Protein (FADD) CLIA Kit Customized Service Offer
n/a ELISA Kit for Fas Associating Death Domain Containing Protein (FADD) ELISA Kit Customized Service Offer
  1. "FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis."Cell 81:505-512(1995) [PubMed] [Europe PMC] [Abstract]
  2. "A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain."J. Biol. Chem. 270:7795-7798(1995) [PubMed] [Europe PMC] [Abstract]
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs." Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
  5. "PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis."Oncogene 18:4409-4415(1999) [PubMed] [Europe PMC] [Abstract]
  6. "LRDD, a novel leucine rich repeat and death domain containing protein."Biochim. Biophys. Acta 1478:280-288(2000) [PubMed] [Europe PMC] [Abstract]
  7. "FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits Fas-mediated Jun NH2-terminal kinase activation."J. Exp. Med. 192:1165-1174(2000) [PubMed] [Europe PMC] [Abstract]
  8. "Fas-associated death domain protein interacts with methyl-CpG binding domain protein 4: a potential link between genome surveillance and apoptosis."Proc. Natl. Acad. Sci. U.S.A. 100:5211-5216(2003) [PubMed] [Europe PMC] [Abstract]
  9. "IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction."Nat. Immunol. 6:981-988(2005) [PubMed] [Europe PMC] [Abstract]
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
  12. "Whole-exome-sequencing-based discovery of human FADD deficiency."Am. J. Hum. Genet. 87:873-881(2010) [PubMed] [Europe PMC] [Abstract]
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
  14. "Initial characterization of the human central proteome."BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
  16. "NMR structure and mutagenesis of the FADD (Mort1) death-effector domain."Nature 392:941-945(1998) [PubMed] [Europe PMC] [Abstract]
  17. "The three-dimensional solution structure and dynamic properties of the human FADD death domain."J. Mol. Biol. 302:171-188(2000) [PubMed] [Europe PMC] [Abstract]
  18. "The structure of FADD and its mode of interaction with procaspase-8."Mol. Cell 22:599-610(2006) [PubMed] [Europe PMC] [Abstract]
  19. "The Fas-FADD death domain complex structure unravels signalling by receptor clustering."Nature 457:1019-1022(2009) [PubMed] [Europe PMC] [Abstract]
  20. "The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations."Nat. Struct. Mol. Biol. 17:1324-1329(2010) [PubMed] [Europe PMC] [Abstract]