Fas (TNFRSF6)-Associated Via Death Domain (FADD) (AA 94-208) antibody
|Synonyms||GIG3, MORT1, MGC8528, Mort1/FADD|
Alternatives Western Blotting (WB), Immunofluorescence (IF)
|5 references available|
|Price||Product not available in this region.|
|Description||During apoptosis, cells exhibit morphological signs of the death process: cell shrinkage, membrane blebbing, and chromatin condensation. The role of the cell surface cytokine receptor, Fas (Apo-1, CD95), in apoptosis has been well characterized. The tumor necrosis factor receptor (TNF-R) can trigger cell death, as well as various other responses. Data suggested that Fas and TNF-R affect a common target in the cell death pathway. This target has been identified as FADD, a novel protein that contains a death domain homologous to the death domains of Fas and TNF-R1. FADD specifically binds to Fas, an association mediated by their homologous death domains. Overexpression of FADD induces apoptosis that is inhibited by CrmA, a poxvirus protein that blocks both Fas- and TNF-induced cell death. Thus, FADD is a central element of the Fas-mediated cell death pathway. This antibody is routinely tested by western blot analysis.|
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
|Molecular Weight||24 kDa|
Related Products: ABIN968533, ABIN967389
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution containing BSA, glycerol.|
|Preservative||0.09% Sodium azide.|
|Storage||Store undiluted at -20°C.|
|Research Area||Cancer, Apoptosis/Necrosis|
|Restrictions||For Research Use only|
|Western blot analysis of FADD on a A431 lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the anti- FADD antibody. Immunoflourescence staining of MDCK cells.|
Chinnaiyan, ORourke, Tewari et al.: "FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis." in: Cell, Vol. 81, Issue 4, pp. 505-12, 1995 (PubMed).
Wieder, Essmann, Prokop et al.: "Activation of caspase-8 in drug-induced apoptosis of B-lymphoid cells is independent of CD95/Fas receptor-ligand interaction and occurs downstream of caspase-3." in: Blood, Vol. 97, Issue 5, pp. 1378-87, 2001 (PubMed).
Chang, Xing, Pan et al.: "c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis." in: The EMBO journal, Vol. 21, Issue 14, pp. 3704-14, 2002 (PubMed).
Micheau, Thome, Schneider et al.: "The long form of FLIP is an activator of caspase-8 at the Fas death-inducing signaling complex." in: The Journal of biological chemistry, Vol. 277, Issue 47, pp. 45162-71, 2002 (PubMed).
MacFarlane, Harper, Snowden et al.: "Mechanisms of resistance to TRAIL-induced apoptosis in primary B cell chronic lymphocytic leukaemia." in: Oncogene, Vol. 21, Issue 44, pp. 6809-18, 2002 (PubMed).