CASP14
CASP14 (caspase 14, also known as MICE) is a cysteine protease of the peptidase C14A family. Unlike most caspases it is non-apoptotic, acting in epidermal differentiation and as the predominant caspase in the epidermal stratum corneum. Browse Assay Genie's current range of CASP14 research reagents below, or read on for the biology behind the target.
CASP14 is a member of the cysteine-aspartic acid protease (caspase) family. Caspases exist as inactive proenzymes that are cleaved at conserved aspartic residues to give large and small subunits, which dimerise to form the active enzyme. Whereas sequential caspase activation drives the execution phase of apoptosis, caspase 14 is classed as a non-apoptotic caspase involved in epidermal differentiation. It is the predominant caspase in the epidermal stratum corneum and appears to play a role in keratinocyte differentiation. It is required for cornification.
Functionally, CASP14 regulates maturation of the epidermis by proteolytically processing filaggrin, and it is involved in processing prosaposin in the epidermis. In vitro it prefers the substrate motif [WY]-X-X-D and is active on the synthetic caspase substrate WEHD-ACF. It is also thought to contribute to DNA degradation in differentiated keratinocytes, probably by cleaving DFFA/ICAD to liberate DFFB/CAD, and it may be involved in retinal pigment epithelium cell barrier function. UniProt reports the protein in the cytoplasm and nucleus.
In vitro, this caspase is processed and activated by caspase 8 and caspase 10, and in vivo by anti-Fas agonist antibody or TNF-related apoptosis inducing ligand. Its expression and processing may be involved in keratinocyte terminal differentiation, which is important for formation of the skin barrier. The CASP14 gene belongs to the HGNC caspase gene group. Earlier names include MICE and caspase 14, apoptosis-related cysteine protease.
CASP14 expression and processing may be involved in keratinocyte terminal differentiation, which is important for formation of the skin barrier.
CASP14 is required for cornification and is the predominant caspase in the stratum corneum, making it central to epidermal maturation studies.
CASP14 proteolytically processes filaggrin and is involved in prosaposin processing in the epidermis, providing a route to study epidermal protein maturation.
CASP14 is processed by caspase 8 and caspase 10 in vitro, linking it to death-receptor signalling such as Fas and TRAIL.
CASP14 is a non-apoptotic caspase involved in epidermal differentiation. It is the predominant caspase in the stratum corneum, is required for cornification, and processes filaggrin to regulate epidermal maturation. It also processes prosaposin and may cleave DFFA/ICAD in differentiated keratinocytes.
The HGNC-approved name is caspase 14. Aliases and previous symbols include MICE, MGC119078 and MGC119079. Earlier names were caspase 14, apoptosis-related cysteine protease, and caspase 14, apoptosis-related cysteine peptidase. UniProt lists the protein as Caspase-14.
A mouse ortholog, Casp14, is recorded in the data; check the datasheet of any product for its validated reactivity. Like other caspases, CASP14 is made as an inactive proenzyme. It is processed by caspase 8 and caspase 10 in vitro, and by anti-Fas agonist antibody or TRAIL in vivo.
Other caspase family members, including the initiator caspases that process CASP14, and related apoptosis-pathway targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P31944; product specifications from Assay Genie datasheets.