Cleaved Caspase-1 (Asp296) Antibody recognizes endogenous levels of Caspase-1 protein only when cleaved at Asp296.

Rat

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asp296 of mouse Caspase-1 protein. Antibodies are purified by protein A and peptide affinity chromatography.

Caspase-1, or interleukin-1ß converting enzyme (ICE/ICEα), is a class I cysteine protease, which also includes caspases -4, -5, -11, and -12. Caspase-1 cleaves inflammatory cytokines such as pro-IL-1ß and interferon-γ inducing factor (IL-18) into their mature forms (1,2). Like other caspases, caspase-1 is proteolytically activated from a proenzyme to produce a tetramer of its two active subunits, p20 and p10. Caspase-1 has a large amino-terminal pro-domain that contains a caspase recruitment domain (CARD). Overexpression of caspase-1 can induce apoptosis (3). Mice deficient in caspase-1, however, have no overt defects in apoptosis but do have defects in the maturation of pro-IL-1β and are resistant to endotoxic shock (4,5). At least six caspase-1 isoforms have been identified, including caspase-1 α, β, γ, δ, ε, and ζ (6). Most caspase-1 isoforms (α, β, γ, and δ) produce products between 30-48 kDa and induce apoptosis upon overexpression. Caspase-1 ε typically contains only the p10 subunit, does not induce apoptosis, and may act as a dominant negative. The widely expressed ζ isoform of caspase-1 induces apoptosis and lacks 39 amino-terminal residues found in the α isoform (6). Activation of caspase-1 occurs through an oligomerization molecular platform designated the "inflammasome" that includes caspase-5, Pycard/Asc, and NALP1 (7).