Anti-Caspase-1

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 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. [The UniProt Consortium]