Preparation And Storage
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.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Companion Products
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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. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
Development References (5)
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Chang DW, Xing Z, Pan Y, et al. c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis. EMBO J. 2002; 21(14):3704-3714. (Biology: Western blot). View Reference
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Chinnaiyan AM, O'Rourke K, Tewari M, Dixit VM. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell. 1995; 81(4):505-512. (Biology). View Reference
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MacFarlane M, Harper N, Snowden RT, et al. Mechanisms of resistance to TRAIL-induced apoptosis in primary B cell chronic lymphocytic leukaemia. Oncogene. 2002; 21(44):6809-6818. (Biology: Western blot). View Reference
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Micheau O, Thome M, Schneider P, et al. The long form of FLIP is an activator of caspase-8 at the Fas death-inducing signaling complex. J Biol Chem. 2002; 277(47):45162-45171. (Biology: Immunoprecipitation, Western blot). View Reference
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Wieder T, Essmann F, Prokop A, 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. Blood. 2001; 97(5):1378-1387. (Biology: Western blot). View Reference
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Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described
Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
