| Species : |
Human |
| Source : |
E.coli |
| Tag : |
His |
| Protein Length : |
2-414 |
| Description : |
Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. Each NADP(+)-dependent isozyme is a homodimer. The protein encoded by this gene is the NADP(+)-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. It contains the PTS-1 peroxisomal targeting signal sequence. The presence of this enzyme in peroxisomes suggests roles in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid. The cytoplasmic enzyme serves a significant role in cytoplasmic NADPH production. Alternatively spliced transcript variants encoding the same protein have been found for this gene. |
| Molecular Mass : |
47.9 kDa |
| Purity : |
≥95% as determined by SDS-PAGE |
| Unit Definition : |
One unit is defined as the amount of enzyme required to convert 1 nmol of NADPH to NADP+, using 15 mM α-ketoglutarate as a substrate, per minute at room temperature in 25 mM Tris-HCl, pH 7.5, 150 mM sodium chloride, and 5 mM MgCl2. |
| Stability : |
≥ 2 years |
| Storage : |
At -80 centigrade. |
| Storage Buffer : |
50 mM Tris-HCl, pH 7.5, containing 200 mM sodium chloride, 5 mM β-mercaptoethanol, and 10% glycerol |