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Carbonic anhydrase III (CAIII) is a member of a multigene family (at least six separate genes are known) that encodes carbonic anhydrase isozymes. Additionally we are shipping Carbonic Anhydrase III Antibodies (85) and Carbonic Anhydrase III Proteins (35) and many more products for this protein.
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After transfer to low carbon dioxide, Cah3 is phosphorylated and phosphorylation is correlated to changes in its localization and its increase in activity.
CO(2) might be generated from HCO(3)(-) by Cah3 in the thylakoid lumen with the following CO(2) diffusion into the pyrenoid, where the CO(2) fixing Rubisco is located.
The results suggest that elevated isoaspartate and CPS-1, and reduced CA-III levels could serve as biomarkers of hepatocellular injury.
During inner ear development, transcripts of four cytosolic isozymes (Car1 (show CA1 ELISA Kits), Car2 (show CA2 ELISA Kits), Car3, and Car13 (show CA13 ELISA Kits)), two membrane-bound isozymes (Car12 and Car14 (show CA14 ELISA Kits)), and two CA-related proteins (Car8 (show CA8 ELISA Kits) and Car11 (show CA11 ELISA Kits)) were expressed at higher levels than other isozymes.
We conclude that down-regulation of CAIII in preadipocytes enhances adipogenesis and that CAIII is a regulator of adipogenic differentiation which acts at the level of PPAR-gamma2 (show PPARG ELISA Kits) gene expression.
Car2, Car3, Car7, and Car15 mRNAs were barely within the detection limits in the mouse harderian gland.
Mice lacking carbonic anhydrase III were viable and fertile and had normal life spans.
lack of proximal tubule cLCN5 in mice and men is associated with CAIII induction, increased cell proliferation, and oxidative stress
this study detected the formation and colocalization of 6-nitrotryptophan-containing proteins and CAIII in the skin of atopic dermatitis patients, not only in the lesional part but also in the nonlesional part, through histochemical analyses
Report that anti-CAIII antibodies may be useful for diagnosing microscopic polyangiitis.
The carbonic anhydrase CA3 isoform displayed an increased abundance during muscle aging, which was independently verified by immunoblotting of differently aged human skeletal muscle samples.
The generation of CA III and IV autoantibodies, antioxidant enzymes, and cytokines might influence each other.
Crystallization and preliminary X-ray analysis of human carbonic anhydrase III
Data show that inserting histidine residues into the active site cavity of carbonic anhydrase II (show CA2 ELISA Kits) or III results in rates of proton transfer to the zinc-bound hydroxide that are antagonistic or suppressive with respect to the corresponding single mutants.
Proton transfer within the active-site cavity of carbonic anhydrase III
myoglobin (show MB ELISA Kits)/carbonic anhydrase III ratio in the blood proved to be a more specific indicator for myocardial damage than myoglobin (show MB ELISA Kits) alone after myocardial infarction.
CAIII expression is upregulated in kidney cortex samples from the end-stage kidney of a patient with Dent's disease owing to the G506E mutation of CLCN5 (show CLCN5 ELISA Kits)
CAIII promotes transformation and invasion capability in hepatoma cells through FAK (show PTK2 ELISA Kits) signaling pathway.
These results demonstrated that CA-III is bound to the transferrin (show Tf ELISA Kits) and albumin (show ALB ELISA Kits), and that its levels were higher in diseased swine compared with the healthy pigs.
Molecular characterization revealed that CA3 genomic DNA consists of seven exons and six introns, spans about 10.5 kb and maps to porcine chromosome 4q11-->q14.
The temporal and spatial distributions of CA3 gene product were analysed and the association between the presence of specific polymorphisms and carcass traits in the pig was also examined.
Carbonic anhydrase III (CAIII) is a member of a multigene family (at least six separate genes are known) that encodes carbonic anhydrase isozymes. These carbonic anhydrases are a class of metalloenzymes that catalyze the reversible hydration of carbon dioxide and are differentially expressed in a number of cell types. The expression of the CA3 gene is strictly tissue specific and present at high levels in skeletal muscle and much lower levels in cardiac and smooth muscle. A proportion of carriers of Duchenne muscle dystrophy have a higher CA3 level than normal. The gene spans 10.3 kb and contains seven exons and six introns.
, carbonate dehydratase III
, carbonic anhydrase III
, carbonic anhydrase 3
, cysteine--tRNA ligase, cytoplasmic
, cysteinyl-tRNA synthetase, cytoplasmic