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AdipoGen Life Sciences
anti-FADD (human), mAb (1C4)
Product Details | |
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Synonyms | FAS-associated Death Domain Protein; Growth-inhibiting Gene 3 Protein; Mediator of Receptor Induced Toxicity; MORT1 |
Product Type | Monoclonal Antibody |
Properties | |
Clone | 1C4 |
Isotype | Mouse IgG1 |
Source/Host | Purified from concentrated hybridoma tissue culture supernatant. |
Immunogen/Antigen | Recombinant human FADD. |
Application |
ELISA Western Blot: (1μg/ml) Immunoprecipitation |
Crossreactivity | Human |
Specificity |
Recognizes the C-terminus of human FADD only in its unphosphorylated form. |
Purity | ≥95% (SDS-PAGE) |
Purity Detail | Protein G-affinity purified. |
Concentration | 1 mg/ml |
Formulation | Liquid. In PBS and 0.02% sodium azide. |
Isotype Negative Control | |
Other Product Data |
UniProt link Q13158: FADD (human) |
Accession Number | Q13158 |
Shipping and Handling | |
Shipping | BLUE ICE |
Short Term Storage | +4°C |
Long Term Storage | -20°C |
Handling Advice |
After opening, prepare aliquots and store at -20°C. Avoid freeze/thaw cycles. |
Use/Stability | Stable for at least 1 year after receipt when stored at -20°C. |
Documents | |
MSDS | Download PDF |
Product Specification Sheet | |
Datasheet | Download PDF |
FADD (FAS-associated death domain protein) is an apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. Procaspase-8 belongs to the family of caspases. Binding of FasL to Fas leads to formation of a receptor complex at the cellular membrane, which was named DISC. The DISC consists of oligomerized receptors, the DD-containing adaptor molecule FADD, procaspase-8, procaspase-10 and c-FLIP. The DISC structure provides a platform for the oligomerization of procaspase-8 that allows two procaspase-8 homodimers to be in the close proximity leading to the initial activation of procaspase-8. FADD is also involved in interferon-mediated antiviral immune response and functions in the positive regulation of interferon signaling. FADD also plays a role in embryonic development and the cell cycle reentry of T cells.
- DEDD, a novel death effector domain-containing protein, targeted to the nucleolus: A.H. Stegh, et al.; EMBO J. 17, 5974 (1998)
- Phosphorylation of FADD/ MORT1 at serine 194 and association with a 70-kDa cell cycle-regulated protein kinase: C. Scaffidi, et al.; J. Immunol. 164, 1236 (2000)
- Phosphorylation of FADD at Serine 194 by CKIα Regulates Its Nonapoptotic Activities: E.C. Alappat, et al.; Mol. Cell 19, 321 (2005)
- CD95 Stimulation Results in the Formation of a Novel Death Effector Domain Protein-containing Complex: I.N. Lavrik, et al.; J. Biol. Chem. 283, 26401 (2008)
- A New C-Terminal Cleavage Product of Procaspase-8, p30, Defines an Alternative Pathway of Procaspase-8 Activation: J.C. Hoffmann, et al.; Mol. Cell. Biol. 29, 4431 (2009)
- Caspase-8 activity has an essential role in CD95/Fas-mediated MAPK activation: A.M.M. Kober, et al.; Cell Death Dis. 2, e212 (2011)
- Modulation of the CD95-Induced Apoptosis: The Role of CD95 N-Glycosylation: O.M. Shatnyeva, et al.; PLoS One 6, e19927 (2011)
- Quantification of High-Molecular Weight Protein Platforms by AQUA Mass Spectrometry as Exemplified for the CD95 Death-Inducing Signaling Complex (DISC): U. Warnken, et al.; Cells 2, 476 (2013)
- Targeting Thioredoxin-1 by dimethyl fumarate induces ripoptosome-mediated cell death: A. Schroeder, et al.; Sci. Rep. 7, 43168 (2017)
- A Dual Role of Caspase-8 in Triggering and Sensing Proliferation-Associated DNA Damage, a Key Determinant of Liver Cancer Development: Y. Boege, et al.; Cancer Cell 32, 342 (2017)
- Delineating the role of c-FLIP/NEMO interaction in the CD95 network via rational design of molecular probes: N.V. Ivanisenko, et al.; BMC Genomics 20, 293 (2019)
- Evaluation of CDK9 Inhibition by Dinaciclib in Combination with Apoptosis Modulating izTRAIL for the Treatment of Colorectal Cancer: X. Shen, et al.; Biomed. 11, 928 (2023)