Anti-IDH1/2 Mutant (R132/172) Antibody, clone MsMab-1

Isocitrate dehydrogenase (IDH) catalyzes the oxidative decarboxylation of isocitrate to produce alpha-ketoglutarate and carbon dioxide. There exist three forms of IDHs in human (IDH1-3), with IDH3 utilizing NAD+ as a cofactor and functioning within the citric acid cycle, while IDH1 (EC 1.1.1.42; UniProt P48735) and IDH2 (EC 1.1.1.42; UniProt P48735) utilizing NADP+ as a cofactor and functioning outside the context of the citric acid cycle. Mutated IDH1 and IDH2 convert alpha-ketoglutarate to oncometabolite R(-)-2-hydroxyglutarate (2-HG) in cytosol and mitochondria, respectively. Isocitrate dehydrogenase 1 ⁄ 2 mutations have been reported in gliomas, acute myeloid leukemias (AMLs), cartilaginous tumors, osteosarcoma, Giant cell tumors of bone (GCTB), Ollier disease, and Maffucci syndrome.

~47 to 50 kDa observed

Epitope: IDH1-R132/IDH2-R172 mutation site

KLH-conjugated peptide derived from human IDH1 sequence with R132G mutation.

Immunohistochemistry Analysis: A 1:50 dilution from a representative lot detected IDH1/2 Mutant (R132/172) in human colon, human colorectal cancer, and human ovarian cancer tissue.
Western Blotting Analysis: The mutant selectivity of a representative lot was tested against purified IDH1/2 MBP fusion constructs as well as lysates from CHO cells expressing exogenously expressed IDH1/2 proteins (Kato Kaneko, M., et al. (2013). Tohoku J Exp Med. 230(2):103-109; Liu, X., et al. (2013). Cancer Med.;2(6):803-814).
Western Blotting Analysis: A representative lot detected exogenously expressed IDH2- R172S, but not wild-type IDH2 or IDH2-H175Y PA fusion proteins in lysates from transfected U2OS osteosarcoma cells (Kato Kaneko, M., et al. (2014). Cancer Sci.;105(6):744-748).
Immunohistochemistry Analysis: A representative lot detected IDH2 R172S mutant, but not wild-type IDH1/2, in paraffin-embedded human GCTB (giant cell tumor of bone) tissue sections (Kato Kaneko, M., et al. (2014). Cancer Sci.;105(6):744-748).
Immunohistochemistry Analysis: A representative lot detected IDH2 R172S mutant, but not wild-type IDH1/2, in paraffin-embedded human osteosarcoma tissue sections (Liu, X., et al. (2013). Cancer Med.;2(6):803-814).

Research Category
Apoptosis & Cancer

Research Sub Category
Apoptosis - Additional

This Anti-IDH1/2 Mutant (R132/172) Antibody, clone MsMab-1 is validated for use in Western Blotting, Immunohistochemistry (Paraffin) for the detection of IDH1/2 Mutant (R132/172).

Clone MsMab-1 recognizes IDH1 with Arg132 mutations (R132AD/E/G/H/M/N/Q/SY) and IDH2 with Arg172 mutations (R172A/C/D/E/G/L/Q/S/Y), but not wild type IDH1/2 or other IDH1/2 mutations (IDH1-R132C/F/I/K/L/P/R/T/V/W; IDH2-H175Y, R172F/H/I/K/M/N/P/T/V/W) by Western blotting and peptide-based ELISA analyses.

Format: Purified

Protein G Purified

Purified mouse monoclonal IgG2aκ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.

Evaluated by Western Blotting in IDH2-R172S-expressing U2OS cell lysate.

Western Blotting Analysis: 2.0 µg/mL of this antibody detected exogenously expressed IDH2-R172S mutant, but not wild-type IDH2, in 10 µg of U2OS cell lysates.

Concentration: Please refer to lot specific datasheet.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.