|Calculated MW||45.9 kDa (384 aa + NT 6xHis-tag)|
|Gene Source||Bacillus Subtilis|
|Storage||-80°C; 2 mg/mL solution in 20 mM Tris, pH 8 containing 20% glycerol.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Oxalate decarboxylase (OxdC, EC18.104.22.168) is a manganese-containing enzyme, which decomposes oxalic acid and oxalate. With OxdC catalysis, oxalate is split into formate and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is oxalate carboxy-lyase (formate-forming). This enzyme is also called oxalate carboxy-lyase. The enzyme is composed of two cupin domains, each of which contains a Mn (II) ion. This enzyme participates in glyoxylate and dicarboxylate metabolism. This enzyme has been recognized for diagnostics in diverse biotechnological applications such as the clinical assay of oxalate in blood and urine, therapeutics, process industry, and agriculture to lower oxalate levels in foods and the environment. The recombinant protein made from the Bacillus Subtilis sequence includes OxdC with N-terminal His-tag.
Wipat A.,et al.Microbiology 144:1593-1600(1998).
Kunst F.,et al.Nature 390:249-256(1997).
Tanner A.,et al.J. Bacteriol. 182:5271-5273(2000).
Tanner A.,et al.J. Biol. Chem. 276:43627-43634(2001).
MacLellan S.R.,et al.Mol. Microbiol. 69:954-967(2008).
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