CA XII polyclonal antibody; host Rabbit; reactivity Human, Mouse, Rat
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carbonic anhydrase 12(CA12) 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. This gene product is a type I membrane protein that is highly expressed in normal tissues, such as kidney, colon and pancreas, and has been found to be overexpressed in 10% of clear cell renal carcinomas. Three transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq, Jun 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,Mouse,Rat |
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Carbonic anhydrase 12 (CA12; carbonic anhydrase XII/CA-XII) is a type I transmembrane zinc metalloenzyme with an extracellular catalytic domain. It is studied in epithelial CO2/bicarbonate handling, extracellular pH regulation and tissue-specific membrane carbonic-anhydrase biology.
Biological function: CA12 catalyses reversible hydration of carbon dioxide at the cell surface, generating bicarbonate and protons and contributing to extracellular acid-base handling. Its transmembrane localisation links carbonic-anhydrase catalysis to epithelial transport and pH-regulatory systems.
