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Merck

I2002

Sigma-Aldrich

Isocitric Dehydrogenase (NADP) from porcine heart

Type IV, buffered aqueous glycerol solution, 3-20 units/mg protein

Sinónimos:

threo-Ds-Isocitrate: NADP+ oxidoreductase, ICDH, IDH

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About This Item

Número de CAS:
Comisión internacional de enzimas:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type IV

Quality Level

form

buffered aqueous glycerol solution

quality

≤ 0.2% of main activity is obtained with NAD as cofactor.

specific activity

3-20 units/mg protein

composition

Protein biuret

shipped in

wet ice

storage temp.

2-8°C

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Application

Isocitric dehydrogenase (IDH) has been used:
  • for in vitro activity assay to study the effects of thorium on citric acid cycle enzymes in the mitochondrial respiration pathway
  • as a standard to measure the impact of temperature on nicotinamide diphosphate (NADP)-IDH activity
  • in isocitrate assay

Biochem/physiol Actions

Isocitrate dehydrogenase (IDH) is a homodimeric enzyme and participates in several processes such as adapting to hypoxia, histone demethylation, and DNA modification. This enzyme has three isoforms like IDH1, IDH2, and IDH3.

Unit Definition

One unit will convert 1.0 μmole of isocitrate to α-ketoglutarate per min at pH 7.4 at 37 °C.

Physical form

Solution in 50% glycerol in EDTA buffer salts, pH 6.0

Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Erdem M Terzi et al.
Science advances, 7(22) (2021-05-28)
Intracellular iron levels are strictly regulated to support homeostasis and avoid iron-mediated ROS production. Loss of iron-sulfur cluster (ISC) synthesis can increase iron loading and promote cell death by ferroptosis. Iron-responsive element-binding proteins IRP1 and IRP2 posttranscriptionally regulate iron homeostasis.
Avtar Singh et al.
The Journal of biological chemistry, 278(35), 33208-33216 (2003-06-07)
Transhydrogenase couples the reduction of NADP+ by NADH to inward proton translocation across mitochondrial and bacterial membranes. The coupling reactions occur within the protein by long distance conformational changes. In intact transhydrogenase and in complexes formed from the isolated, nucleotide-binding
Icksoo Lee et al.
Biochimica et biophysica acta, 1802(2), 275-283 (2009-10-20)
Noonan syndrome (NS) is an autosomal dominant disorder, and a main feature is congenital heart malformation. About 50% of cases are caused by gain-of-function mutations in the tyrosine phosphatase SHP2/PTPN11, a downstream regulator of ERK/MAPK. Recently it was reported that
M Ryan Smith et al.
Redox biology, 8, 136-148 (2016-01-18)
Many cancer cells follow an aberrant metabolic program to maintain energy for rapid cell proliferation. Metabolic reprogramming often involves the upregulation of glutaminolysis to generate reducing equivalents for the electron transport chain and amino acids for protein synthesis. Critical enzymes
Sergiy M Nadtochiy et al.
The Journal of biological chemistry, 291(38), 20188-20197 (2016-08-12)
2-Hydroxyglutarate (2-HG) is an important epigenetic regulator, with potential roles in cancer and stem cell biology. The d-(R)-enantiomer (d-2-HG) is an oncometabolite generated from α-ketoglutarate (α-KG) by mutant isocitrate dehydrogenase, whereas l-(S)-2-HG is generated by lactate dehydrogenase and malate dehydrogenase

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