CA I polyclonal antibody; host Rabbit; reactivity Human, Rat, Mouse
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carbonic anhydrase 1(CA1) Homo sapiens Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva and gastric acid. They show extensive diversity in tissue distribution and in their subcellular localization. This CA1 gene is closely linked to the CA2 and CA3 genes on chromosome 8. It encodes a cytosolic protein that is found at the highest level in erythrocytes. Allelic variants of this gene have been described in some populations. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2014],
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 | IHC-P | IF | ELISA |
|---|---|---|---|---|
| Human,Rat,Mouse |
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Carbonic anhydrase 1 (CA1; carbonic anhydrase I/CA-I, also CAB) is a cytosolic zinc metalloenzyme that catalyses reversible carbon dioxide hydration. It is especially abundant in erythrocytes and is studied in CO2 transport, bicarbonate chemistry and systemic acid-base physiology.
Biological function: CA1 catalyses the reversible interconversion of carbon dioxide and water with bicarbonate and protons through a zinc-containing active site. This rapid reaction supports carbon dioxide handling and proton/bicarbonate balance; its high erythrocyte abundance makes CA1 useful for studying carbonic-anhydrase catalysis and red-cell gas and acid-base chemistry.
