Anti-Caspase-1

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Caspase-1, an apoptosis-related cysteine protease, 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 was purified from the cytosol of the THP monocytic cell line and found that the active protease was made up of two peptides, which they called p20 and p10 based on their apparent molecular masses by SDS-PAGE. It belongs to a family of cysteine proteases known as caspases that always cleave proteins following an aspartic acid residue. The CASP1 gene 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 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]