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Description
IDH1(R132C) His Tag Protein, HumanProduct Specification Species Human Synonyms IDH1, PICD, IDP Accession O75874 1 Amino Acid Sequence Met 1 Leu 414 with His Tag at the C Terminus Expression System E. coli Molecular Weight 40 55kDa (Reducing) Purity 95% by SDS PAGE & HPLC Conjugation Unconjugated Tag His Tag Physical Appearance Liquid Storage Buffer 50mM Tris, 150mM NaCl, pH7. 5, 1mM DTT, 10%Glycerol Stability & Storage Stable for 12 months upon stored at 80 from the date of receipt.
Product Specification
| Species | Human |
| Synonyms | IDH1, PICD, IDP |
| Accession | O75874-1 |
| Amino Acid Sequence | Met 1-Leu 414 with His Tag at the C-Terminus |
| Expression System | E.coli |
| Molecular Weight | 40-55kDa (Reducing) |
| Purity | ＞95% by SDS-PAGE & HPLC |
| Conjugation | Unconjugated |
| Tag | His Tag |
| Physical Appearance | Liquid |
| Storage Buffer | 50mM Tris, 150mM NaCl, pH7.5, 1mM DTT, 10%Glycerol |
| Stability & Storage | Stable for 12 months upon stored at -80℃ from the date of receipt. |
| Reference | 1. Parsons, D.W., et al. (2008). An integrated genomic analysis of human glioblastoma multiforme. Science, 321(5897), 1807-1812. |
Background
IDH1 (Isocitrate Dehydrogenase 1) is a key metabolic enzyme located in the cytoplasm and peroxisomes. Its primary physiological function is to catalyze the oxidative decarboxylation of isocitrate to produce alpha-ketoglutarate (α-KG), while concurrently reducing NADP+ to NADPH. This reaction is crucial for cellular metabolism, as it links the tricarboxylic acid (TCA) cycle with lipid metabolism and provides NADPH, a major reducing agent essential for antioxidant defense and anabolic biosynthesis.
A seminal discovery in cancer biology revealed that specific heterozygous somatic mutations in the IDH1 gene, most commonly at the R132 residue, are frequent drivers in several cancers. These include gliomas (especially secondary glioblastoma and oligodendroglioma), acute myeloid leukemia (AML), cholangiocarcinoma, and chondrosarcomas. The mutant enzyme acquires a neomorphic activity: instead of producing α-KG, it reduces α-KG to D-2-hydroxyglutarate (D-2HG). This oncometabolite, D-2HG, accumulates to high levels and functions as a competitive inhibitor of multiple α-KG-dependent dioxygenases. This inhibition leads to profound epigenetic dysregulation (via inhibition of histone and DNA demethylases) and blockade of cellular differentiation, thereby promoting tumorigenesis.
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