|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 (PubMed:9827558, PubMed:11744710, PubMed:19864430). Can also oxidize the herbicide glyphosate (N-phosphonomethylglycine) (PubMed:19864430). Displays lower activities on D-alanine, D- valine, D-proline and D-methionine (PubMed:9827558, PubMed:11744710). Does not act on L-amino acids and other D-amino acids (PubMed:9827558). 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 (PubMed:12627963).|
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Provided below are standard protocols that you may find useful for product applications.
Glycine oxidase (GO) from Bacillus subtilis (EC 126.96.36.199) 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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