Caspase 1 (cleaved Asp297) Antibodies

Target Information

Caspase 1 (cleaved Asp297) encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. Caspase 1 (cleaved Asp297) was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in the processes such as inflammation, septic shock, and wound healing. Caspase 1 (cleaved Asp297) has been shown to induce cell apoptosis and may function in various developmental stages. Studies of a similar gene in mouse suggest a role in the pathogenesis of Huntington disease. Alternative splicing results in transcript variants encoding distinct isoforms.

Synonyms

CASP1; CASP-1; CASP1 nirs variant 1; caspase 1; caspase 1, apoptosis-related cysteine peptidase (interleukin 1, beta, convertase); caspase-1; Caspase-1 subunit p10; Caspase-1 subunit p20; ICE; IL-1 beta-converting enzyme; IL1BC; IL-1BC; IL1BCE; IL1B-convertase; interleukin 1, beta, convertase; interleukin 1-B converting enzyme; Interleukin-1 beta convertase; Interleukin-1 beta-converting enzyme; p45