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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. Zusätzlich bieten wir Ihnen Carbonic Anhydrase III Kits (33) und Carbonic Anhydrase III Proteine (29) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 117 products:
Human Monoclonal CA3 Primary Antibody für IHC (p), ELISA - ABIN560131
Doran, Wilton, Fletcher, Ohlendieck: Proteomic profiling of antisense-induced exon skipping reveals reversal of pathobiochemical abnormalities in dystrophic mdx diaphragm. in Proteomics 2009
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Human Polyclonal CA3 Primary Antibody für WB - ABIN391954
Du, Ren, Lu, Tu, Xu, Sun: Carbonic anhydrase III is insufficient in muscles of myasthenia gravis patients. in Autoimmunity 2009
Show all 2 Pubmed References
Human Polyclonal CA3 Primary Antibody für IHC, IHC (p) - ABIN4287740
Bachmann, Burté, Pramana, Conte, Brown, Orimadegun, Ajetunmobi, Afolabi, Akinkunmi, Omokhodion, Akinbami, Shokunbi, Kampf, Pawitan, Uhlén, Sodeinde, Schwenk, Wahlgren, Fernandez-Reyes, Nilsson: Affinity proteomics reveals elevated muscle proteins in plasma of children with cerebral malaria. in PLoS pathogens 2014
CAIII and Hsp70 expressions were higher in LPRD patients that in non-LPRD patients, suggesting the possibility as one of biomomarker in LPRD diagnosis.
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 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/carbonic anhydrase III ratio in the blood proved to be a more specific indicator for myocardial damage than myoglobin 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
CAIII promotes transformation and invasion capability in hepatoma cells through FAK signaling pathway.
The level of CAIII is specifically insufficient in the skeletal muscle of myasthenia gravis patients.
CrCAH3 has unique structural features that allow this enzyme to maximize photosystem II activity at low pH and carbon dioxide concentration.
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.
CAIII is highly expressed in osteocytes, is regulated by parathyroid hormone both in vitro and in vivo, and protects osteocytes from oxidative stress.
Our results indicate that Car3 is not required for de novo lipogenesis, and Car3 knockout mice fed high-fat diet do not have significant differences in responses to various diets to wild type mice.
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, Car2, Car3, and Car13), two membrane-bound isozymes (Car12 and Car14), and two CA-related proteins (Car8 and Car11) 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 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
These results demonstrated that CA-III is bound to the transferrin and albumin, 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 3
, carbonic anhydrase III
, carbonic anhydrase III, muscle specific