Anti-Caspase-1 (Clone: ABM1B93)

Caspase-1 is a member of the cysteine-aspartic acid protease (caspase) family, which acts as a proinflammatory caspase whose catalytic activity is tightly regulated by signal-dependent autoactivation within inflammasomes. Caspase-1 is produced as a zymogen that is 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 interacts with another CARD domain containing protein called PYCARD (or ASC) and is involved in inflammasome formation and activation of inflammatory processes. Inflammasome-dependent caspase-1 activity results in a highly inflammatory form of cell death known as pyroptosis, primarily described in myeloid cells infected with intracellular bacterial pathogens. caspase-1 is implicated in promoting CD4 T-cell death and inflammation by HIV, two signature events that fuel HIV disease progression to AIDS. Protein function: Thiol protease that cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. Important for defense against pathogens. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Can also promote apoptosis. Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive (PubMed:28314590). [The UniProt Consortium]