Anti-Caspase-1 (p20)

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Caspase-1 is a cysteine protease that regulates inflammatory processes through its capacity to process and activate the interleukin-1-beta, IL-18, and IL-33 precursor proteins. It belongs to a family of cysteine proteases known as caspases that always cleave proteins following an aspartic acid residue. The Caspase-1 gene consists of 10 exons spanning at least 10.6 kb and is mapped to 11q23, a site frequently involved in rearrangement in human cancers, including a number of leukemias and lymphomas, by Southern DNA blot analysis of rodent-human hybrids and by in situ hybridization to normal human metaphase chromosomes. Caspase 1 has been shown to induce cell necrosis or pyroptosis and may function in various developmental stages. Protein function: Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins, such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D (GSDMD), into active mature peptides (PubMed:21147462, PubMed:32109412). Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex, it initiates a pro-inflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18, releasing the mature cytokines which are involved in a variety of inflammatory processes (PubMed:21147462). Cleaves a tetrapeptide after an Asp residue at position P1 (PubMed:21147462). Also initiates pyroptosis, a programmed lytic cell death pathway, through cleavage of GSDMD (PubMed:32109412). In contrast to cleavage of interleukin IL1B, recognition and cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part (PubMed:32109412). Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (PubMed:18667412, PubMed:22464733, PubMed:35705808). 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). In apoptotic cells, cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly. [The UniProt Consortium]