Glutamate dehydrogenase, Recombinant: >300 U/mg,
Size: 100mg
Catalogue Number: NATE-1145
Citations, Manuals and MSDS Available upon request.
Product Description: Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate.
Storage: 4°C, store at -20°C for long-term preservation.
Applications: Except glutamate dehydrogenation, GLDH can also catalytic the deaminase of other amino acids such as L-valine, L-2-aminobutyric acid and L-leucine. The main measuring method is continuous monitoring. Moreover, GLDH catalyzes the reaction of α-ketoglutarate, H+, ammonia and NADH to generating glutamic. Since NADH is the color source of many biochemical assays, therefore the reaction catalyzed by the corresponding GLDH is widely used to detect the final step of biochemical detection reagent.
Activity: 58 u/mg protein
CAS#: 9001-46-1
Research Use Only