CA III polyclonal antibody; host Rabbit; reactivity Human, Mouse, Rat
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carbonic anhydrase 3(CA3) Homo sapiens 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. [provided by RefSeq, Oct 2008],
Fully tested in-house by ABMIUM, or supported by an advanced validation report from a partner reviewed by ABMIUM. Highest confidence. Non-conformities fully supported under the ABMIUM Product Promise.
Quality verified. Independent collaborator or expected-performance data available. Product meets ABMIUM quality standards.
Expected to work based on structural and biochemical data. Not yet directly tested by ABMIUM or a collaborator. No non-conformity support for this combination.
Not recommended for this application or species/sample combination. This may indicate either evidence of unsuitability or that the combination has not been tested and therefore cannot currently be recommended.
Evidence status by application and model.
| Species / reactivity | WB | ELISA |
|---|---|---|
| Human,Mouse,Rat |
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Carbonic anhydrase 3 (CA3; carbonic anhydrase III/CA-III) is a cytosolic zinc metalloenzyme with carbonic-anhydrase activity and strong tissue enrichment in skeletal muscle. It is studied in muscle physiology, isozyme-specific CO2 hydration and carbonic-anhydrase expression biology.
Biological function: CA3 catalyses reversible hydration of carbon dioxide using a zinc cofactor. It is distinguished from other carbonic-anhydrase isozymes by tissue-specific expression, including high abundance in skeletal muscle, making it useful for studies of muscle-associated carbonic-anhydrase biology and isozyme kinetics.
