CASP4
CASP4 (caspase 4, also known as ICE(rel)II, ICH-2 and TX) is a cysteine-aspartic acid protease of the peptidase C14A family. It can cleave and activate its own precursor and the caspase 1 precursor, and it is linked to apoptosis and inflammasome-associated pyroptosis. Browse Assay Genie's current range of CASP4 research reagents below, or read on for the biology behind the target.
CASP4 belongs to the cysteine-aspartic acid protease (caspase) family, in which sequential activation plays a central role in the execution phase of apoptosis. Like other caspases, it exists as an inactive proenzyme made up of a prodomain and large and small protease subunits. Activation requires proteolytic processing at conserved internal aspartic residues, producing a heterodimeric enzyme of large and small subunits. CASP4 can cleave and activate its own precursor as well as the caspase 1 precursor, and when overexpressed the CASP4 gene induces apoptosis.
Caspase-4 is placed in the peptidase C14A family and is annotated in the HGNC caspase and caspase recruitment domain containing gene groups. UniProt records it in the cytosol, at the endoplasmic reticulum membrane, in the mitochondrion, in the inflammasome and as a secreted protein. Alternative splicing of the gene gives transcript variants that encode distinct isoforms. The mouse ortholog is Casp4.
In a microbial infection context, caspase-4 is activated by cathepsin G (CTSG) in response to the Td92 surface protein of the periodontal pathogen T. denticola. This leads to production and secretion of IL1A and to pyroptosis of gingival fibroblasts. The protein has also been catalogued as apoptosis-related cysteine protease or peptidase, and under the aliases ICE(rel)II, ICH-2 and TX, so literature searches often need several names.
CASP4 is a caspase whose overexpression induces apoptosis, making it relevant to studies of the caspase activation cascades that drive cell death.
Caspase-4 is localised to the inflammasome and is linked to pyroptosis, so it is a focus for research on inflammatory cell death.
CASP4 cleaves and activates its own precursor and the caspase 1 precursor, which makes it useful for dissecting caspase processing steps.
Caspase-4 activation by cathepsin G in response to T. denticola Td92 drives IL1A secretion, relevant to periodontal infection research.
CASP4 is a cysteine-aspartic acid protease that cleaves and activates its own precursor and the caspase 1 precursor. Overexpression induces apoptosis. In response to T. denticola Td92, cathepsin G activates it, leading to IL1A secretion and pyroptosis of gingival fibroblasts.
Aliases include ICE(rel)II, ICH-2 and TX. Earlier HGNC names were caspase 4, apoptosis-related cysteine protease and caspase 4, apoptosis-related cysteine peptidase. UniProt calls the protein Caspase-4. Alternative splicing produces transcript variants that encode distinct isoforms.
A mouse ortholog, Casp4, is recorded for the human gene. CASP4 sits in the peptidase C14A family alongside other caspases. Check the datasheet of any product for its validated reactivity before using it with mouse or other samples.
Other caspases, including inflammatory and apoptotic family members, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P49662; product specifications from Assay Genie datasheets.