CASP7
CASP7 (caspase 7, also known as MCH3, CMH-1 and ICE-LAP3) is a member of the cysteine-aspartic acid protease family that acts in the execution phase of apoptosis. It is made as an inactive proenzyme and activated by proteolytic processing in response to cell death stimuli. Browse Assay Genie's current range of CASP7 research reagents below, or read on for the biology behind the target.
CASP7 encodes a cysteine-aspartic acid protease, or caspase. Sequential activation of caspases plays a central role in the execution phase of cell apoptosis. Like other family members, caspase-7 exists as an inactive proenzyme. Proteolytic processing at conserved aspartic residues produces a large and a small subunit, and these dimerise to form the active enzyme. The precursor of the encoded protein is cleaved by caspase 3 and caspase 10, is activated upon cell death stimuli and induces apoptosis.
Caspase-7 belongs to the peptidase C14A family and is classed in the HGNC caspase gene group. The enzyme is assigned EC 3.4.22.60. UniProt reports its subcellular locations as the cytosol, the nucleus and the extracellular space. The mouse ortholog is Casp7, which allows the pathway to be studied in murine systems. The UniProt function annotation also records that a form of the protein lacks enzymatic activity, so the form under study is worth defining in any experiment.
The CASP7 gene is alternatively spliced, and RefSeq notes multiple transcript variants encoding different isoforms. This matters when choosing a CASP7 antibody or other detection reagent, because the precursor, the processed subunits and the isoforms differ in size and in what they represent. Reagents are usually chosen to tell the inactive proenzyme from the cleaved, active form.
The protein has gone by several names. Aliases include MCH3, CMH-1 and ICE-LAP3, and earlier HGNC names described it as an apoptosis-related cysteine protease or peptidase. Other caspases, such as caspase-3, caspase-6, caspase-8 and caspase-9, work in the same apoptotic cascade, so CASP7 is often examined alongside them.
CASP7 acts in the execution phase of apoptosis, so it is a standard readout of programmed cell death in cell and tissue models.
Caspase-7 is cleaved by caspase 3 and caspase 10, making it useful for mapping the order of caspase activation.
Cleavage at conserved aspartic residues converts the inactive precursor into large and small subunits that dimerise into the active enzyme.
Alternative splicing yields multiple CASP7 isoforms, and UniProt notes a form lacking enzymatic activity, which makes isoform-specific study relevant.
CASP7 encodes caspase-7, a cysteine-aspartic acid protease that functions in the execution phase of apoptosis. It is produced as an inactive proenzyme, cleaved into large and small subunits that dimerise, and activated upon cell death stimuli, where it induces apoptosis.
Aliases are MCH3, CMH-1 and ICE-LAP3, and older names include caspase 7, apoptosis-related cysteine protease. RefSeq reports alternatively spliced transcript variants encoding multiple isoforms. UniProt also notes a form lacking enzymatic activity, so check which isoform is relevant to your work.
A mouse ortholog, Casp7, is recorded for this gene. In humans the precursor is cleaved by caspase 3 and caspase 10 to give the active enzyme. Check the datasheet of any product for its validated reactivity before use in a given species.
Other caspases, including executioner and initiator family members and apoptosis pathway partners with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P55210; product specifications from Assay Genie datasheets.