Caspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis. The precursor form of all caspases is composed of a prodomain, and large and small catalytic subunits. The active forms of caspases are generated by several stimuli including ligand-receptor interactions, growth factor deprivation and inhibitors of cellular functions. All known caspases require cleavage adjacent to aspartates to liberate one large and one small subunit, which associate into tetramer to form the active enzyme. Caspase-1/ICE (IL-1b converting enzyme) is similar to the cell death gene CED-3 of Caenorhabditilis elegans and regulates multiple proinflammatory cytokines, including interleukin-1b and interferon-gamma-inducing factor. Caspase 1, also called interleukin-1 beta converting enzyme, is a cysteine C14 endopeptidase able to process pro-interleukin-1 beta into its active form. Caspase 1 is identical to Caenorhabditis elegans cell death gene ced-3 and may be involved in apoptotic signalling. Inhibition of caspase-1 in mice models extended survival and delayed appearance of neuronal inclusions and symptoms of Huntingdon disease.
Caspase-1 antibody can be used in ELISA, Western Blot, and immunohistochemistry starting at 5 μg/mL.
Protein G Column
PBS, 0.2% gelatin, 0.05% sodium azide.
Aliquot and store at -20°C. Avoid multiple freeze-thaw cycles.
Reactivity: Gibbon, Gorilla, Human