This gene encodes a member of the cysteine-aspartic acid protease (caspase) family of enzymes. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic acid residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspases 7, 8 and 10, and is thought to function as a downstream enzyme in the caspase activation cascade. Alternative splicing of this gene results in multiple transcript variants that encode different isoforms.
Caspase-7, also named as CMH-1, Mch3 and ICE-LAP3, has been identified as a major contributor to the execution of apoptosis. Caspase-7, like caspase-3, is an effector caspase that is responsible for cleaving downstream substrates such as ADP-ribose polymerase and PARP. During apoptosis, caspase-7 is activated through proteolytic processing by upstream caspases at Asp23, Asp198, and Asp206 to produce the mature subunits. Similar to caspase-2 and -3, caspase-7 preferentially cleaves substrates following the recognition sequence DEVD.
Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death.
Caspase 8,also named as MCH5,MACH,FLICE,and CAP4,belongs to the peptidase C14A family. It may participate in the GZMB apoptotic pathways and functions as an upstream regulator in a-bisabolol-induced apoptosis. Caspase 8 catalyzes an essential intermediate step in the ubiquitination and proteasome-mediated degradation of IRF3. It may control diabetic embryopathy-associated apoptosis via Caspase 8 is expressed as nine isoforms by alternative splicing with the molecular mass from 26 kDa to 62 kDa. Caspase 8 Monoclonal Antibody can recognize pro- and cleaved-caspase 8.
This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases.
Caspase 9,apoptosis-related cysteine protease (CASP9,synonyms: MCH6,APAF3,APAF-3,ICE-LAP6,CASPASE-9c)is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits,large and small,that dimerize to form the active enzyme. Capase 9 is processed by caspase APAF1; this step is thought to be one of the earliest in the caspase activation cascade.
This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein can undergo autoproteolytic processing and activation by the apoptosome, a protein complex of cytochrome c and the apoptotic peptidase activating factor 1; this step is thought to be one of the earliest in the caspase activation cascade. This protein is thought to play a central role in apoptosis and to be a tumor suppressor. Alternative splicing results in multiple transcript variants.
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