Caspase-1 (interleukin-1 beta convertase) belongs to the Interleukin-1-beta converting enzyme subfamily of caspases which mediate many 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. Caspase-1 promotes maturation of interleukin IL-1 beta and interleukin 18 (IL-18) by proteolytic cleavage of precursor forms into biologically active pro-inflammatory cytokines. Cleavage of Caspase-1 into the p20 and p10 subunits directly correlates with the progression of apoptosis in the cell resulting in the initiation of the caspase cascade. Proteolytic cleavage of the precursor caspase-1 at glycine residue 317 in human and 315 in mouse generates the functional caspase-1 subunits, known as p20 and p10 subunits. At the amino acid level, the mouse p10 subunit is 81% identical to the human p10 subunit.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
