Caspase 1, apoptosis-related cysteine protease, is a cysteine protease that regulates inflammatory processes through its capacity to process and activate the interleukin-1-beta, IL18 , and IL33 precursor proteins. Caspase 1 was purified ICE from the cytosol of the THP.1 human monocytic cell line and found that the active protease was made up of 2 peptides, which they called p20 and p10 based on their apparent molecular masses by SDS-PAGE.It belongs to a family of cysteine proteases known as caspases that always cleave proteins following an aspartic acid residue. The Caspase1 gene consists of 10 exons spanning at least 10.6 kb. The Caspase 1 gene is mapped to 11q23, a site frequently involved in rearrangement in human cancers, including a number of leukemias and lymphomas, by Southern DNA blot analysis of rodent-human hybrids and by in situ hybridization to normal human metaphase chromosomes. Caspase 1 has been shown to induce cell necrosis or pyroptosis and may function in various developmental stages.