CASP12
CASP12 (inactive caspase-12, previously CASP12P1) is a member of the caspase family that may act as a negative regulator of inflammatory responses and innate immunity. In most humans the gene encodes a truncated, non-functional protein. Browse Assay Genie's current range of CASP12 research reagents below, or read on for the biology behind the target.
Caspases are cysteine proteases that cleave C-terminal aspartic acid residues on their substrate molecules. CASP12 belongs to the peptidase C14A family and is most closely related to the ICE subfamily of caspases, which process inflammatory cytokines. Unlike its relatives, human CASP12 may lack protease activity. UniProt annotates it as a possible negative regulator of inflammatory responses and innate immunity, which may reduce cytokine release in response to bacterial lipopolysaccharide during infection and reduce activation of NF-kappa-B in response to TNF.
The human CASP12 gene carries a polymorphism for the presence or absence of a premature stop codon. Most individuals carry the stop codon and produce a truncated, non-functional protein. The read-through form occurs primarily in individuals of African descent, and carriers show endotoxin hypo-responsiveness and increased susceptibility to severe sepsis. Several alternatively spliced transcript variants have been noted for the gene.
The rodent homologue, Casp12 in mouse and rat, is reported to mediate apoptosis in response to endoplasmic reticulum stress, which marks a clear functional difference from the human protein. HGNC classifies the gene within the caspases and the caspase recruitment domain containing groups, and its earlier names, caspase 12 pseudogene 1 and CASP12P1, reflect the frequent loss of function in humans. This makes CASP12 a useful subject for comparative work on caspase evolution and inflammatory regulation.
CASP12 may act as a negative regulator of innate immune responses, including cytokine release after bacterial lipopolysaccharide exposure.
The read-through allele is linked to endotoxin hypo-responsiveness and increased susceptibility to severe sepsis in carriers.
CASP12 reduces activation of NF-kappa-B in response to TNF, making it relevant to inflammatory signalling research.
The human stop-codon polymorphism and the rodent role in endoplasmic reticulum stress apoptosis support cross-species comparisons.
UniProt describes CASP12 as a possible negative regulator of inflammatory responses and innate immunity. It may reduce cytokine release in response to bacterial lipopolysaccharide and reduces NF-kappa-B activation in response to TNF. It may lack protease activity, so its role appears regulatory.
CASP12P1 and caspase 12 pseudogene 1 are previous HGNC names. They reflect that most humans carry a premature stop codon and produce a truncated, non-functional protein, hence the UniProt name inactive caspase-12. Several alternatively spliced transcript variants have also been noted.
Mouse and rat both have a Casp12 ortholog. In rodents it mediates apoptosis in response to endoplasmic reticulum stress, while the human protein is usually non-functional. The read-through allele is linked to endotoxin hypo-responsiveness and increased susceptibility to severe sepsis. Check the datasheet of any product for its validated reactivity.
Other caspases, including inflammatory and apoptotic family members, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q6UXS9; product specifications from Assay Genie datasheets.