Caspase-1
Caspase-1 (CASP1) is a cysteine-aspartic acid protease of the caspase family, also known as ICE and IL1BC. It was identified by its ability to cleave and activate the inactive precursor of interleukin-1, linking apoptosis machinery to inflammatory cytokine processing. Browse Assay Genie's current range of Caspase-1 research reagents below, or read on for the biology behind the target.
Caspase-1 is a member of the cysteine-aspartic acid protease (caspase) family, which plays a central role in the execution phase of apoptosis through sequential caspase activation. Like other caspases, it exists as an inactive proenzyme. Proteolytic processing at conserved aspartic acid residues produces a large and a small subunit, and these dimerise to form the active enzyme. Caspase-1 is annotated as belonging to the peptidase C14A family.
The Caspase-1 gene was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in processes such as inflammation, septic shock and wound healing. This activity gave the protein its original name, interleukin-1 beta convertase (ICE), and the alias IL1BC. The Caspase-1 gene has also been shown to induce apoptosis and may function at various developmental stages. The protein localises to the cytoplasm and the cell membrane, and alternative splicing of the gene produces transcript variants that encode distinct isoforms.
HGNC places CASP1 in the caspase group and in the group of caspase recruitment domain (CARD) containing proteins. Earlier approved names described it as an apoptosis-related cysteine protease or peptidase and as an interleukin 1, beta, convertase. Studies of a similar gene in mouse, Casp1, suggest a role in the pathogenesis of Huntington disease. Rat also has a Casp1 ortholog, so the protein can be studied in common rodent models.
Caspase-1 cleaves and activates the interleukin-1 precursor, making it central to studies of inflammatory cytokine processing.
As a caspase that can induce apoptosis, Caspase-1 is studied within the sequential proenzyme activation cascades of cell death.
Interleukin-1 activation by Caspase-1 connects the protease to septic shock and wound healing, two processes the cytokine influences.
Work on the mouse Casp1 gene suggests a role in Huntington disease pathogenesis, supporting use in neurodegeneration studies.
Caspase-1 is a cysteine protease that proteolytically cleaves and activates the inactive precursor of interleukin-1, a cytokine involved in inflammation, septic shock and wound healing. It has also been shown to induce apoptosis and may function in various developmental stages.
Caspase-1 is encoded by CASP1 and is also called ICE (interleukin-1 beta convertase) and IL1BC. Alternative splicing produces transcript variants that encode distinct isoforms, so check the datasheet of any product for its validated reactivity and isoform coverage.
Mouse and rat both have a Casp1 ortholog. Studies of a similar gene in mouse suggest a role in the pathogenesis of Huntington disease. Check the datasheet of any product for its validated reactivity before using it in another species.
Other caspase family members and apoptosis-pathway proteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P29466; product specifications from Assay Genie datasheets.