Recombinant CASP1 protein (His tag)

• DataSheet
• Material Safety Data Sheets (MSDS)

Recombinant Caspase-1 (CASP-1) Fragment (residues 131-285) is a highly purified, stable protein segment derived from human Caspase-1, a key enzyme in inflammatory and immune responses. This 155-amino acid fragment is optimized for solubility and structural integrity, making it an ideal tool for biochemical assays, structural studies, and inflammasome research.

Caspase-1, also known as interleukin-1 beta convertase (ICE), is a thiol protease central to inflammatory processes. It functions by proteolytically cleaving precursors of inflammatory cytokines such as interleukin-1 beta (IL1B) and interleukin-18 (IL18) into their active forms, initiating pro-inflammatory responses. Additionally, Caspase-1 triggers pyroptosis, a lytic cell death pathway, through cleavage of Gasdermin-D (GSDMD), and it plays roles in antiviral immunity and plasma membrane repair via cleavage of CGAS and CASP7, respectively. The protein is primarily localized in the cytoplasm and cell membrane, where it becomes activated within inflammasome complexes to drive immune and cell death signaling pathways.