caspase-1 p10 Anticorpo (M-20): sc-514

Caspase-1, originally designated ICE (for IL-1 converting enzyme), is a member of the group of caspases with large prodomains. Caspase-1 promotes maturation of interleukin IL-1 beta and interleukin18 (IL-18) by proteolytic cleavage of precursor forms into biologically active pro-inflamatory cytokines. The prodomain of caspase-1 (also known as Pro-C1) represents the amino acid terminal portion of the caspase-1 precursor. Pro-C1 is produced as a residual component after proteolytic cleavage of the precursor generates the functional caspase-1 subunits known as the p20 and p10 subunits. Active caspase-1, a (p20/p10)2 tetramer, is necessary and sufficient for cleavage of precursor IL-1 as well as for induction of apoptosis in some cell lines. The highly conserved family of caspases mediate many of the morphological and biochemical features of apoptosis, including structural dismantling of cell bodies and nuclei, fragmentation of genomic DNA, destruction of regulatory proteins and propagation of other pro-apoptotic molecules. The human Caspase-1 gene maps to chromosome 2q14 and encodes a cytoplasmic protein expressed in liver, heart, skeletal muscle kidney and testis. Caspase-1 has been implicated in inflammation, septic shock, and other situations such as wound healing and the growth of certain leukemias.