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Caspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis (1). 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 a 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.
Casp1; CASP-1; CASP1 nirs variant 1; caspase 1; caspase 1, apoptosis-related cysteine peptidase (interleukin 1, beta, convertase); caspase-1; Caspase-1 subunit p10; Caspase-1 subunit p20; ICE; IL-1 beta converting enzyme; IL-1 beta-converting enzyme; IL-1B converting enzyme; Il1bc; IL-1BC; IL1BCE; IL1B-convertase; interleukin 1 beta-converting enzyme; interleukin 1, beta, convertase; interleukin 1-B converting enzyme; interleukin-1 beta convertase; interleukin-1 beta converting enzyme; Interleukin-1 beta-converting enzyme; P45
100 µg
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