IDH1 Antibody (YA3565)

IDH1 (isocitrate dehydrogenase 1) is a cytosolic and peroxisomal NADP⁺-dependent enzyme that catalyzes the conversion of isocitrate to α-ketoglutarate (α-KG) while generating NADPH, thereby supporting cellular redox homeostasis and intermediary metabolism^[1][2]. Mechanistically, IDH1 contributes to metabolic pathways that regulate oxidative stress responses, biosynthetic processes, and α-KG availability for multiple cellular reactions^[1][2]. In cancer biology, IDH1 is notable because recurrent mutations, most commonly affecting residue R132, confer a neomorphic enzymatic activity that converts α-KG into D-2-hydroxyglutarate (D-2HG), an oncometabolite that accumulates in tumor cells^[3][2][4]. Elevated D-2HG inhibits α-KG-dependent dioxygenases, resulting in widespread epigenetic alterations and impaired cellular differentiation that contribute to tumor development and progression^[2][4][5]. These molecular effects have been extensively studied in glioma and acute myeloid leukemia models, where mutant IDH1 functions as an early driver of tumorigenesis and metabolic reprogramming^[4][5][6]. Compared with the related isoform IDH2, which is localized primarily in mitochondria, IDH1 is predominantly cytosolic and peroxisomal, creating distinct subcellular metabolic functions despite sharing similar catalytic chemistry^[1][7]. For experimental applications, selective mutant IDH1 inhibitors reduce D-2HG production and promote cellular differentiation in preclinical models, making them valuable tools for investigating IDH1-dependent metabolic and epigenetic mechanisms in cancer research^[5][6][8].