Caspase-1/CASP1 p20 Protein, Human (GST)

Caspase-1/CASP1 subunit p10 Protein, a thiol protease, intricately participates in various inflammatory processes by catalyzing the proteolytic cleavage of precursor proteins associated with inflammation. This includes interleukin-1 beta (IL1B) and interleukin 18 (IL18), pivotal inflammatory cytokines, as well as the pyroptosis inducer Gasdermin-D (GSDMD), converting them into active mature peptides. Functioning as a key initiator of cell immunity, Caspase-1 activates a pro-inflammatory response upon inflammasome complex formation, leading to the release of mature cytokines IL1B and IL18, which play critical roles in diverse inflammatory pathways. Caspase-1's activity extends to initiating pyroptosis, a programmed lytic cell death pathway, by cleaving GSDMD. Notably, unlike its cleavage of interleukins, the recognition and cleavage of GSDMD depend on an exosite interface on CASP1, emphasizing its versatile and complex regulatory roles. Moreover, Caspase-1 activates CASP7 in response to bacterial infection, promoting plasma membrane repair, and controls antiviral immunity by cleaving CGAS upon inflammasome activation during DNA virus infection. In apoptotic cells, Caspase-1 cleaves SPHK2, which remains enzymatically active extracellularly. Despite its involvement in diverse cellular processes, Caspase-1 is apoptosis inactive.