Anti-Caspase-1 (CASP1) antibody is validated on mouse tissue and recommended for immunofluorescence labeling, IHC, or western blot of materials from rodent and human tissues.
Caspase-1/Interleukin-1 converting enzyme (ICE) is a cysteine-aspartic acid protease that is encoded by the CASP1 gene in human. Caspase-1 plays a central role in cell immunity as an inflammatory response initiator. Once activated through formation of an inflammasome complex, it initiates a proinflammatory response through the cleavage and thus activation of the two inflammatory cytokines, interleukin 1β (IL-1β) and interleukin 18 (IL-18), as well as pyroptosis, a programmed lytic cell death pathway, through cleavage of Gasdermin D.
Caspase-1 is produced as a zymogen that can then be cleaved into 20 kDa (p20) and 10 kDa (p10) subunits that become part of the active enzyme. Active Caspase-1 contains two heterodimers of p20 and p10. It contains a catalytic domain with an active site that spans both the p20 and p10 subunits, as well as a noncatalytic Caspase Activation and Recruitment Domain (CARD).
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