|Application ||WB, E|
|Other Accession||NP_001729, 759, 12346 (mouse), 310218 (rat)|
|Calculated MW||28870 Da|
|Other Names||Carbonic anhydrase 1, 220.127.116.11, Carbonate dehydratase I, Carbonic anhydrase B, CAB, Carbonic anhydrase I, CA-I, CA1|
|Format||0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Goat Anti-CA1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea.|
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Provided below are standard protocols that you may find useful for product applications.
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. CA1 is closely linked to CA2 and CA3 genes on chromosome 8, and it encodes a cytosolic protein which is found at the highest level in erythrocytes. Variants of this gene have been described in some populations. Multiple alternatively spliced variants, encoding the same protein, have been identified. Transcript variants of CA1 utilizing alternative polyA_sites have been described in literature.
Diabetic retinopathy is not associated with carbonic anhydrase gene polymorphisms. Abhary S, et al. Mol Vis, 2009 Jun 13. PMID 19536309.
Toward a confocal subcellular atlas of the human proteome. Barbe L, et al. Mol Cell Proteomics, 2008 Mar. PMID 18029348.
Decreased total carbonic anhydrase esterase activity and decreased levels of carbonic anhydrase 1 isozyme in erythrocytes of type II diabetic patients. Gambhir KK, et al. Biochem Genet, 2007 Jun. PMID 17464559.
Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I. Temperini C, et al. Bioorg Med Chem Lett, 2007 Apr 15. PMID 17314045.
Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I. Temperini C, et al. Bioorg Med Chem Lett, 2006 Oct 1. PMID 16870440.
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