Apo D-Amino Acid Oxidase

<strong>Apo D-Amino Acid Oxidase</strong>_x000D_ <strong>Catalog number:</strong> B2013291_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 1000 U_x000D_ <strong>Molecular Weight or Concentration:</strong> 25-30 U/mg protein_x000D_ <strong>Supplied as:</strong> Powder_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -20C_x000D_ <strong>Keywords:</strong> Apo D-Amino Acid Oxidase_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Marcotte P, Walsh C. Vinylglycine and proparglyglycine: complementary suicide substrates for L-amino acid oxidase and D-amino acid oxidase Biochemistry. 1976 Jul 13;15(14):3070-6._x000D_ 2: Stocker A, Hecht HJ, Bückmann AF. Synthesis, characterization and preliminary crystallographic data of N6-(6-carbamoylhexyl)-FAD-D-amino-acid oxidase from pig kidney, a semi-synthetic oxidase Eur J Biochem. 1996 Jun 1;238(2):519-28._x000D_ 3: Pollegioni L, Simonetta MP. Immunochemical studies on Rhodotorula gracilis D-amino acid oxidase Experientia. 1991 Mar 15;47(3):232-5._x000D_ 4: Casalin P, Pollegioni L, Curti B, Pilone Simonetta M. A study on apoenzyme from Rhodotorula gracilis D-amino acid oxidase Eur J Biochem. 1991 Apr 23;197(2):513-7._x000D_ 5: Schräder T, Andreesen JR. Studies on the inactivation of the flavoprotein D-amino acid oxidase from Trigonopsis variabilis Appl Microbiol Biotechnol. 1996 May;45(4):458-64._x000D_ 6: YAGI K, OZAWA T. Binding of the sulphydryl group in D-amino-acid oxidase apo-protein with flavin adenine dinucleotide Nature. 1959 Oct 17;184(Suppl 16):1227-8._x000D_ 7: Pollegioni L, Ceciliani F, Curti B, Ronchi S, Pilone MS. Studies on the structural and functional aspects of Rhodotorula gracilis D-amino acid oxidase by limited trypsinolysis Biochem J. 1995 Sep 1;310 ( Pt 2)(Pt 2):577-83._x000D_ 8: Soltysik S, Byron CM, Einarsdottir GH, Stankovich MT. The effects of reversible freezing inactivation and inhibitor binding on redox properties of L-amino-acid oxidase Biochim Biophys Acta. 1987 Jan 30;911(2):201-8._x000D_ 9: YAGI K, HARADA M. Binding site of flavin adenine dinucleotide combining with sulphydryl group of D-amino-acid oxidase apo-enzyme Nature. 1962 Jun 23;194:1179-80._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/1979077">10: Tarelli GT, Vanoni MA, Negri A, Curti B. Characterization of a fully active N-terminal 37-kDa polypeptide obtained by limited tryptic cleavage of pig kidney D-amino acid oxidase J Biol Chem. 1990 Dec 5;265(34):21242-6.</a>_x000D_ _x000D_ <strong>Products Related to Apo D-Amino Acid Oxidase can be found at</strong> <a href="https://moleculardepot.com/product-category/Enzymes/"> Enzymes</a>