Anti-IDH2 (mutated R172W) antibody [WMab-1]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Isocitrate dehydrogenase 2 (IDH2) is an enzyme that converts isocitrate to alpha-ketoglutarate in the citric acid cycle through oxidative decarboxylation. IDH2 also known as NADP-dependent isocitrate dehydrogenase has a molecular weight of about 51 kDa. This protein expresses in the mitochondria serving an important role in cellular energy production and intermediary metabolism. By facilitating this conversion IDH2 impacts cellular respiration and energy balance.

Biological function summary

The IDH2 enzyme facilitates cellular metabolism by producing NADPH critical for biosynthesis and antioxidant defense. It functions within the oxidative decarboxylation of isocitrate providing reducing equivalents to keep cellular redox balance. Although not part of a larger enzymatic complex IDH2 acts synergistically with other metabolic enzymes to maintain cellular biochemical pathways.

Pathways

The IDH2 protein participates in the citric acid cycle and redox homeostasis. IDH2 contributes to the tricarboxylic acid (TCA) pathway coupling with other TCA components such as citrate synthase and aconitase. Within the redox pathway it influences glucose metabolism via its link with enzymes like NADPH oxidase ensuring a steady supply of NADPH for biosynthetic reactions.

Associated diseases and disorders

The IDH2 protein links to certain cancers like acute myeloid leukemia (AML) due to mutations such as IDH2 R140Q and IDH2 R172K which lead to the production of oncometabolite 2-hydroxyglutarate. This oncometabolite influences epigenetic regulation and cellular differentiation. IDH2 mutations often associate with altered tumor suppressor pathways involving proteins like TP53 contributing to tumorigenesis and impaired cellular differentiation.