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Cat No.
NATE-1103
Description
Isocitrate dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms:IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead of NAD+. They localize to the cytosol as well as the mitochondrion and peroxisome.
Abbr
IDH, Recombinant (Bacillus subtilis)
Alias
IDH
Species
Bacillus subtilis
Form
In 3.2 M ammonium sulphate.
Enzyme Commission Number
EC 1.1.1.42
Bio-activity
12.9 U/mg protein at pH 7.6 and 25°C.
Molecular Mass
~ 48,581
Isoelectric point
~ 5.4
Unit Definition
One Unit of isocitrate dehydrogenase is defined as the amount of enzyme required to produce one μmole of NADPH from NADP+.
Optimum pH
7.6
Thermal stability
up to 25°C
Stability
> 2 years at 4°C
Preparation Instructions
For assay, this enzyme should be diluted in 200 mM Tris.HCl buffer, pH 7.6 containing 10 mM MgCl2 and 1 mg/ml BSA. Swirl to mix the enzyme suspension immediately prior to use.
Applications
High purity recombinant Isocitrate dehydrogenase (B. subtilis) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
Synonyms
Isocitrate Dehydrogenase (NADP+); EC 1.1.1.42; IDH; Isocitrate Dehydrogenase; NADP-dependent isocitric dehydrogenase; NADP-linked isocitrate dehydrogenase; NADP-specific isocitrate dehydrogenase; Oxalosuccinate decarboxylase; Oxalsuccinic decarboxylase; Triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase
