Invitrogen™ Caspase 1 p20 (Cleaved Asp296) Polyclonal Antibody

Caspase-1 p20 (cleaved Asp296) refers to the large catalytic subunit generated during activation of pro-caspase-1, an inflammatory cysteine protease encoded by the CASP1 gene. Caspase-1 is synthesized as an inactive zymogen and becomes activated within multiprotein inflammasome complexes in response to infection, cellular stress, or danger-associated signals. Activation involves autoproteolytic cleavage at specific aspartic acid residues, including at Asp296, producing the p20 (large) and p10 (small) subunits that assemble into the active heterotetrameric enzyme. The p20 fragment contains part of the catalytic domain and is commonly used as a marker of caspase-1 activation. Active caspase-1 mediates the proteolytic maturation of pro-inflammatory cytokines such as interleukin-1β (IL-1β) and interleukin-18 (IL-18) and drives pyroptosis, an inflammatory form of programmed cell death. Detection of cleaved caspase-1 p20 (Asp296) is therefore widely used to assess inflammasome activation in immunology and inflammation research.