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G1924-1UN
PLN 588.00
G1924-5UN
PLN 1,970.00
PLN 588.00
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About This Item
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recombinant
expressed in E. coli
Quality Level
form
solid
specific activity
≥5 units/mg protein
mol wt
120 kDa
storage temp.
−20°C
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This Item | G1270 | G5921 | C8649 |
|---|---|---|---|
| specific activity ≥5 units/mg protein | specific activity 400-2,000 units/mg protein | specific activity ≥5.0 units/mg solid | specific activity ≥20 units/mg protein |
| recombinant expressed in E. coli | recombinant - | recombinant expressed in E. coli | recombinant - |
| form solid | form lyophilized powder | form lyophilized powder | form lyophilized powder |
| storage temp. −20°C | storage temp. −20°C | storage temp. 2-8°C | storage temp. −20°C |
| mol wt 120 kDa | mol wt - | mol wt - | mol wt ~34 kDa |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
General description
L-Glutamate Oxidase (LGOX) from Streptomyces sp is secreted extracellularly in the wheat bran pre cultivation medium. It corresponds to a molecular weight of 120 kDa with monomer subunit of 61 kDa.[1] The structure of LGOX comprises of hexamer and has flavin adenine dinucleotide prosthetic group.[2]
This product has a 6xHistidine tag with a thrombin cleavage site.
Application
Biochem/physiol Actions
Other Notes
One unit will form 1.0 micromole of alpha-ketoglutaric acid from L-glutamic acid per minute at pH 7.4 at 30 deg C.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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L-Glutamate biosensor based on l-glutamate oxidase immobilized onto ZnO nanorods/polypyrrole modified pencil graphite electrode
Batra B, et al.
Biochemical Engineering Journal, 105, 428-436 (2016)
Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G
Wachiratianchai S, et al.
Electronic journal of Biotechnology, 7(3), 09-10 (2004)
Comparative study of hydrogel-immobilized L-glutamate oxidases for a novel thick-film biosensor and its application in food samples
Kwong AWK, et al.
Biotechnology Letters, 22(4), 267-272 (2000)
Jiro Arima et al.
The FEBS journal, 276(14), 3894-3903 (2009-06-18)
L-Glutamate oxidase (LGOX) from Streptomyces sp. X-119-6, which catalyzes the oxidative deamination of L-glutamate, has attracted increasing attention as a component of amperometric L-glutamate sensors used in the food industry and clinical biochemistry. The precursor of LGOX, which has a
Andrea C Kneuttinger et al.
Cell chemical biology, 26(11), 1501-1514 (2019-09-10)
Imidazole glycerol phosphate synthase (ImGPS) is an allosteric bienzyme complex in which substrate binding to the synthase subunit HisF stimulates the glutaminase subunit HisH. To control this stimulation with light, we have incorporated the photo-responsive unnatural amino acids phenylalanine-4'-azobenzene (AzoF)
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