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- Email: info@nsjbio.com
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Caspase 1, apoptosis-related cysteine protease, is a cysteine protease that regulates inflammatory processes through its capacity to process and activate the interleukin-1-beta, IL18, and IL33 precursor proteins. Caspase 1 was purified ICE from the cytosol of the THP. human monocytic cell line and found that the active protease was made up of 2 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 Caspase1 gene consists of 10 exons spanning at least 10.6 kb. The Caspase 1 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 human metaphase chromosomes. Caspase 1 has been shown to induce cell necrosis or pyroptosis and may function in various developmental stages.
Optimal dilution of the Caspase 1 antibody should be determined by the researcher.
E. coli-derived recombinant human protein (amino acids N132-H404) was used as the immunogen for the Caspase 1 antibody.
After reconstitution, the Caspase 1 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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