Glutamate Dehydrogenase (GDH) produced recombinantly in E. coli.
GDH is an oxidoreductase enzyme which relates carbon and nitrogen metabolism. It catalyzes the reduction of α-ketoglutarate and ammonia to L-glutamate and vice versa. This enzyme is a robust and ideal candidate for research use, and industrial applications in the diagnostics and food industries.
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|Name:||Glutamate dehydrogenase (GDH)|
|Source:||E. coli(recombinant enzyme from a thermophilic bacterium)|
|Molecular Weight:||270 kDa; Homohexameric ( 45 kDa per subunit)|
|Buffer:||0.05 M Tris base and 0.5 M NaCl (before lyophilizing)|
|Stability:||At -20ºC, it keeps 100% of its activity after one year|
|Concentration:||> 13% (w/w)|
|Activity:||> 90 U/mg protein; One unit is defined as the conversion of 1?mol of ?-ketoglutarate into glutamate, in 1 minute at 50°C at pH 8.0|
|Temperature Range:||20-70ºC (optimal: 50ºC)|
|pH Range:||7-8.5 (optimal: 8)|
|Storage:||At -20 ºC|
Research and Diagnostics:
Glutamate dehydrogenase activity at different temperatures
Swissaustral GDH is more stable than GDH from bovine liver sources in a broad spetrum of temperatures offering close tooptimal activity between 30C and 70C.
If you publish research with this product, please let us know so we can cite your paper.