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Aspergillus niger gox Recombinant Protein (N-His) (JN979012)

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Overview
Catalog No.JN979012
Description
Recombinant Aspergillus niger gox Protein, N-His (JN979012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% as determined by SDS-PAGE.
Expression systemE. coli
AccessionP13006
Protein lengthSer23-Gln605
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesAspergillus niger
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Reconstitution Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate NamesBeta-D-glucose:oxygen 1-oxido-reductase, EC:1.1.3.4, GOD, GOx, Glucose oxidase, gox
Background

Glucose oxidase is a ~65 kDa protein. Glucose oxidase catalyzes the oxidation of beta-D-glucose to D-glucono-delta-lactone and hydrogen peroxide in the presence of molecular oxygen. D-glucono-delta-lactone is sequentially hydrolyzed by lactonase to D-gluconic acid, and the resulting hydrogen peroxide is hydrolyzed by catalase to oxygen and water (PubMed:14188176, PubMed:14257628, PubMed:14299649, PubMed:15450808, PubMed:2076553, PubMed:2406261, PubMed:24283586, PubMed:28631058, PubMed:28939970, PubMed:34500289, PubMed:7826581, Ref.4, Ref.5). The activity shows high specificity to beta-D-glucose, with very low to no activity towards L-glucose, 2-deoxy-D-glucose, 3-deoxy-D-glucose, 4-deoxy-D-glucose, 5-deoxy-D-glucose, 6-deoxy-D-glucose, 3-O-methyl-D-glucose, 4-O-methyl-D-glucose, 6-O-methyl-D-glucose, 4,6-O-benzylidene-D-glucose, 5-thio-5-deoxy-D-glucose, D-mannose, D-allose, D-galactose, D-fructose, D-arabinose, D-xylose, trehalose, melibiose, L-mannomethylose, lactose, sucrose or 1,5-anhydro-D-glucitol (PubMed:14188176, PubMed:14257628, PubMed:24283586, Ref.5).

1. PAZUR, JH. et al. (1964) Biochemistry 3, 578-83. PMID: 14188176
2. GIBSON, QH. et al. (1964) The Journal of biological chemistry 239, 3927-34. PMID: 14257628
3. SWOBODA, BE. et al. (1965) The Journal of biological chemistry 240, 2209-15. PMID: 14299649
4. Karmali, K. et al. (2004) Analytical biochemistry 333, 320-7. PMID: 15450808
5. Whittington, H. et al. (1990) Current genetics 18, 531-6. PMID: 2076553
6. Frederick, KR. et al. (1990) The Journal of biological chemistry 265, 3793-802. PMID: 2406261
7. Meng, Y. et al. (2014) Letters in applied microbiology 58, 393-400. PMID: 24283586
8. Khadivi Derakshan, F. et al. (2017) Molecular biotechnology 59, 307-314. PMID: 28631058
9. Zhu, X. et al. (2018) Biotechnology letters 40, 103-110. PMID: 28939970
10. Zhong, P. et al. (2022) Food chemistry 370, 130901. PMID: 34500289
Note For research use only
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