Clone: FLICE 1 1-37
Background: Caspases are key effectors of programmed cell death. They are synthesized as inactive proenzymes which are activated by cleavage at a specific aspartate residue to form two subunits. These subunits are normally linked together by a linker which may be involved in the regulation of the different caspases. Caspase-8 is a key enzyme in the apoptosis pathway. Caspase-8 contains two N-terminal region death effector domains which are removed to activate the enzyme along with cleavage into the two subunits. These subunits then for the active protease which is capable of cleaving caspase-3, -6 and -7. These caspases are then capable of cleaving other cellular substrates such as PARP and DFF, which in turn induce apoptosis.
Positive Control: MCF-7 cell lysates
Immunogen: Hybridoma produced by the fusion of splenocytes from mice immunized with recombinant human capase-8 protein and mouse myeloma cells.
Purification Method: Protein A/G Chromatography
Concentration: See vial for concentration
Formulation: Provided as solution in phosphate buffered saline with 0.08% sodium azide
References: 1. Cohen, G.M., et al. Caspases: the executioners of apoptosis. Biochem. J. 1997, 326, 1-162. Martin, D.A., et al. Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal. J. Biol. Chem. 1998, 273, 4345-43493. Green, D.R., Apoptotic pathways: the roads to ruin. Cell 1998, 94, 695-6984. Hu, S., et al. I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1- and CD-95-induced apoptosis. J. Biol. Chem. 1997, 272, 17255-17257
UniProt: Q14790
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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