The isocitrate dehydrogenase 2 (IDH2) gene encodes a metabolic enzyme localized in the mitochondrial matrix, playing a critical role in the tricarboxylic acid (TCA) cycle by catalyzing the oxidative decarboxylation of isocitrate to α-ketoglutarate (α-KG). Mutations in IDH2. particularly at residues R140 and R172. are recurrently observed in cancers such as gliomas, acute myeloid leukemia (AML), and chondrosarcomas. These gain-of-function mutations confer neomorphic activity, enabling the enzyme to reduce α-KG to the oncometabolite D-2-hydroxyglutarate (2-HG), which disrupts cellular epigenetics and redox homeostasis, promoting tumorigenesis. IDH2 antibodies are essential tools for detecting IDH2 protein expression, mutation status, and subcellular localization in research and diagnostics. They are widely used in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to study IDH2's role in cancer metabolism and to identify patients with IDH2-mutant tumors. Clinically, IDH2 mutation detection using specific antibodies or sequencing guides therapeutic decisions, as mutant IDH2 inhibitors (e.g., enasidenib) have been approved for AML treatment. The development and validation of IDH2 antibodies require careful specificity testing due to high homology with IDH1. a cytoplasmic isoform. These antibodies continue to advance precision oncology and mechanistic studies of metabolic dysregulation in cancer.