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MABC1103

Sigma-Aldrich

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

clone MsMAb-1, from mouse

Synonym(s):

Isocitrate dehydrogenase [NADP] cytoplasmic, IDH, Cytosolic NADP-isocitrate dehydrogenase, IDP, NADP(+)-specific ICDH, Oxalosuccinate decarboxylase, Isocitrate dehydrogenase [NADP], mitochondrial, ICD-M

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

MsMAb-1, monoclonal

species reactivity

human

technique(s)

immunohistochemistry: suitable (paraffin)
western blot: suitable

isotype

IgG2aκ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

General description

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.

Specificity

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.

Immunogen

Epitope: IDH1-R132/IDH2-R172 mutation site
KLH-conjugated peptide derived from human IDH1 sequence with R132G mutation.

Application

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).

Quality

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.

Target description

~47 to 50 kDa observed

Physical form

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.

Storage and Stability

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

Other Notes

Concentration: Please refer to lot specific datasheet.

Disclaimer

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.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Establishment of a multi-specific monoclonal antibody MsMab-1 recognizing both IDH1 and IDH2 mutations.
Kato Kaneko, M; Ogasawara, S; Kato, Y
The Tohoku Journal of Experimental Medicine null
Isocitrate dehydrogenase 2 mutation is a frequent event in osteosarcoma detected by a multi-specific monoclonal antibody MsMab-1.
Liu, X; Kato, Y; Kaneko, MK; Sugawara, M; Ogasawara, S; Tsujimoto, Y; Naganuma et al.
Cancer Medicine null
Isocitrate dehydrogenase mutation is frequently observed in giant cell tumor of bone.
Kato Kaneko, M; Liu, X; Oki, H; Ogasawara, S; Nakamura, T; Saidoh, N; Tsujimoto et al.
Cancer Science null
Shuai Chen et al.
Cell death & disease, 9(3), 347-347 (2018-03-03)
WW domain-binding protein 2 (WBP2) has been demonstrated as oncogenic in breast cancer. Many studies have revealed the WBP2 gene as a high-risk gene for leukoariaosis and cerebral white matter lesions is important in the pathologic stage of glioma development.
Marion Classe et al.
Cell reports, 25(3), 811-821 (2018-10-18)
Esthesioneuroblastoma (ENB) is a rare cancer of the olfactory mucosa, with no established molecular stratification to date. We report similarities of ENB with tumors arising in the neural crest and perform integrative analysis of these tumors. We propose a molecular-based

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