A high-sensitive HMab-2 specifically detects IDH1-R132H, the most common IDH mutation in gliomas

Yuki Fujii, Satoshi Ogasawara, Hiroharu Oki, Xing Liu, Mika K. Kaneko, Shingo Takano, Yukinari Kato

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)


Isocitrate dehydrogenase 1 (IDH1) mutations have been detected in gliomas and other tumors. Although IDH1 catalyzes the oxidative carboxylation of isocitrate to α-ketoglutarate (α-KG) in cytosol, mutated IDH1 proteins possess the ability to change α-KG into the oncometabolite D-2-hydroxyglutarate (D-2HG). Several monoclonal antibodies (mAbs) specific for IDH1 mutations have been established, such as H09, IMab-1, and HMab-1 against IDH1-R132H, which is the most frequent IDH1 mutation in gliomas. In this study, we established a novel high-sensitive mAb HMab-2, which reacts with IDH1-R132H but not with wild type IDH1 in ELISA. HMab-2 reacted only with IDH1-R132H, not with wild type IDH1/2 and other IDH1/2 mutants in Western-blot analysis. Furthermore, HMab-2 recognized IDH1-R132H more sensitively compared with our previously established HMab-1. HMab-2 detected endogenous IDH1-R132H protein expressed in glioblastoma in immunohistochemical analysis. HMab-2 is expected to be useful for the diagnosis of IDH1-R132H-bearing tumors.

Original languageEnglish
Pages (from-to)733-739
Number of pages7
JournalBiochemical and biophysical research communications
Issue number4
Publication statusPublished - 2015 Oct 30


  • HMab-2
  • IDH1
  • IDH1 mutation
  • Monoclonal antibody
  • R132H

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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