|Calculated MW||40937 Da|
|Positive Control||WB: r Glycine Oxidase|
|Application & Usage||WB: 1-4 µg|
|Other Names||Glycine oxidase, glycine oxygen oxidoreductase (deaminating), GO|
|Formulation||In PBS pH 7.2, 0.01 % BSA, 0.03 % ProClin® and 50 % glycerol|
|Reconstitution & Storage||-20 °C|
|Precautions||Glycine Oxidase Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha- keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes sarcosine (N-methylglycine), N-ethylglycine and glycine. Can also oxidize the herbicide glyphosate (N-phosphonomethylglycine). Displays lower activities on D-alanine, D-valine, D-proline and D- methionine. Does not act on L-amino acids and other D-amino acids. Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine intermediate (dehydroglycine) required for the biosynthesis of the thiazole ring of thiamine pyrophosphate.|
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Provided below are standard protocols that you may find useful for product applications.
Glycine oxidase (GO) from Bacillus subtilis (EC 22.214.171.124) is a homotetrameric flavin-dependent oxidoreductase. Each GO monomer is non-covalently bound to flavin adenine dinucleotide. GO catalyzes oxidative deamination of various primary and secondary amines (e.g. glycine, sarcosine, N-ethylglycine) and some D-amino acids (e.g. D -alanine, D -proline, D -valine) to the corresponding α-keto acids and hydrogen peroxide. Primarily, glycine oxidase catalyzes the oxidation of glycine in the biosynthesis of thiamine. The variant H244K shows a higher substrate specificity ratio for glycine versus sarcosine and a 5-fold improved specific activity in comparison to the wild-type.
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