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C1099 Sigma

Caspase 8 human

≥90% (SDS-PAGE), recombinant, expressed in E. coli (C-terminal histidine tagged), buffered aqueous solution, ≥1,000 units/mg protein

Synonym: FLICE, MASH, Mch5

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Properties

Related Categories Apoptosis Enzymes, Apoptosis and Cell Cycle, Application Index, Biochemicals and Reagents, Caspase 8,
recombinant   expressed in E. coli (C-terminal histidine tagged)
assay   ≥90% (SDS-PAGE)
form   buffered aqueous solution
mol wt   mol wt ~30 kDa
shipped in   dry ice
storage temp.   −70°C
Gene Information   human ... CASP8(841)

Description

Packaging

10 μg in poly bottle

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.

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.

General description

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.

Price and Availability


All labs need water

Biomedical Applications
Safety & Documentation

Safety Information

Symbol 
Signal word 
Danger
Hazard statements 
Precautionary statements 
RIDADR 
NONH for all modes of transport
WGK Germany 
2
Protocols & Articles
Peer-Reviewed Papers
15

References

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