Human recombinant C−terminal histidine tagged caspase 8 is expressed as the truncated pro-caspase 8 (amino acids 213−496). It is a fully active protein consisting of 18 kDa and 12.4 kDa subunits; the 12.4 kDa subunit contains the histidine tag.
Biochem/physiol Actions
Caspase 8 is at the top of the hierarchy of the caspase cascade and is considered an initiator caspase. It exists in the cell as an inactive 55 kDa proenzyme. It is converted to the active form, consisting of 18 kDa and 11 kDa subunits, upon its recruitment to the cytoplasmic domain of activated death receptors such as CD95 or TNFR via the adapter protein FADD. The activation of the proenzyme is triggered by the protein′s aggregation, which leads to auto- or transprocessing. Caspase 8 activates downstream caspases (caspases 3, 6, and 7) that cleave key cellular substrates and lead to apoptotic death of the cells.
Unit Definition
One unit will cleave 1.0 nmol of Ac-Ile-Glu-Thr-Asp-pNA per min at pH 7.4 at 25 °C.
Physical form
Solution in 10% sucrose containing 20 mM Tris-HCl, 150 mM imidazole-HCl, pH 8.0, 20 mM 2-mercaptoethanol, 500 mM NaCl, 2.5 mM EDTA, and 0.1% CHAPS.
BH3 interacting-domain death agonist (Bid) is a BH3-only pro-apoptotic member of the Bcl-2 family of proteins. Its function in apoptosis is associated with the proteolytic cleavage to the truncated form tBid, mainly by caspase-8. tBid translocates to mitochondria and assists
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