Background
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.

Antigen
A synthetic peptide corresponding to amino acids 31-45 QTRVLNKEEMEKVKR of human Caspase-1 was used as immunogen. The antibody will cross-react with mouse Caspase-1, based on NCBI BLAST.

Application Notes
In HeLa, a 45 kDa band is observed. The antibody recognizes full-length Caspase-1.  The antibody also recognizes cleaved caspase-1 forms that include amino acids 31-45 of the Caspase-1 protein. 

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Reference
1. Cerretti DP, et al. Science 256:97-100 (1992).
2. Yuan J, et al. Cell 75: 641-652 (1993).
3. Li PH, et al. Cell 80:401-411 (1995).
4. Tatsuta T. et al. J. Bio.Chem. 275:14248-54 (2000).