The Caspases are a family of cysteine proteases that induce apoptosis in response to a variety of intra- and extracellular stimuli. These enzymes are synthesized as inactive precursors which become cleaved at aspartate-specific sites upon induction of apoptosis2. Caspase 1 (ICE) is found in many cell types and is predominantly localized to the cytosol and to a lesser extent on the cell surface membrane3. It was originally identified for facilitating apoptosis via cleavage of pro-IL-1beta into the mature and active form and during CD95-induced cell death3-5. Moreover, additional studies have linked Caspase 1 to inflammation through its activation of several cytokine pathways including IL-1beta and IL-18, as well as to septic shock3,6,7. The SB122a monoclonal antibody detects a band at ~45 kD, corresponding to the full length form of Caspase 1.
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