BD Pharmingen™ Purified Mouse Anti-Human FADD
Clone A66-2 (RUO)
Western blot analysis of FADD. Daudi B lymphoma cell lysate was probed with anti-human FADD (clone A66-2, Cat. No. 65751A) at concentrations of 2.0 (lane 1), 1.0 (lane 2), and 0.5 µg/ml (lane 3). The antibody identifies FADD as an ~27 kDa band.
Western blot analysis of FADD. Daudi B lymphoma cell lysate was probed with anti-human FADD (clone A66-2, Cat. No. 65751A) at concentrations of 2.0 (lane 1), 1.0 (lane 2), and 0.5 µg/ml (lane 3). The antibody identifies FADD as an ~27 kDa band.
Preparation And Storage
Recommended Assay Procedures
Clone A66-2 can be used for western blot analysis (1-2 µg/ml). Other reported applications not routinely tested at BD Biosciences include immunoprecipitation (1-2 µg/1x10^6 cells). Daudi B lymphoma cells (ATCC CCL-213) are suggested as a positive control.
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- 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.
FADD is a molecule involved in the Fas-mediated cell death pathway. Apoptosis is induced when Fas ligand or agonistic Fas antibodies bind to the Fas receptor, and trigger the activation of a cell death signaling pathway. Induction of Fas-mediated apoptosis requires a conserved cytoplasmic motif, referred to as the death domain, that is present in the C-terminal end of Fas. FADD also contains a death domain, and Fas and FADD bind to each other through their respective death domains. Death domains are thought to act as adaptor proteins by linking Fas and other members of the tumor necrosis factor receptor (TNFR) superfamily to downstream signaling pathways. Overexpression of FADD in vitro leads to cell death suggesting that FADD, like FAS, is an apoptosis-inducing protein. The N-terminal, but not the C-terminal death domain, is required for apoptosis induced by FADD overexpression. It is thought that the amino-terminal region of FADD functions by binding to caspase-3 and thereby linking signals from the cell surface to an apoptopic protease cascade. FADD has a calculated molecular weight of 24 kDa and migrates at a molecular weight of ~27 kDa in SDS/PAGE.
Development References (2)
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Cleveland JL, Ihle JN. Contenders in FasL/TNF death signaling. Cell. 1995; 81(4):479-482. (Biology). View Reference
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Muzio M, Chinnaiyan AM, Kischkel FC, et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex. Cell. 1996; 85(6):817-827. (Biology).
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For Research Use Only. Not for use in diagnostic or therapeutic procedures.