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SAB4200548

Sigma-Aldrich

Anti-IDH1 (R132H) antibody, Mouse monoclonal

clone HMab-1, purified from hybridoma cell culture

Synonym(s):

Idh1 R132H Antibody, Idh1 R132H Antibody - Anti-IDH1 (R132H) antibody, Mouse monoclonal, Anti-IDCD, Anti-IDH, Anti-IDP, Anti-IDPC, Anti-Isocitrate dehydrogenase 1 (NADP+), soluble, Anti-NADP(+)-specific ICDH, Anti-NADP-dependent isocitrate dehydrogenase, cytosolic, Anti-NADP-dependent isocitrate dehydrogenase, peroxisomal, Anti-Oxalosuccinate decarboxylase, Anti-PICD

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

HMab-1, monoclonal

form

buffered aqueous solution

mol wt

antigen ~43 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

western blot: 4.0-8.0 μg/mL using extract of HEK-293T cells overexpressing IDH1R132H.

UniProt accession no.

application(s)

research pathology

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... IDH1(3417)

General description

Anti-IDH1 (R132H) antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the hybridoma HMab1 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a peptide corresponding to mutation R132H of human IDH1. A member of isocitrate dehydrogenase (IDH) family, IDH1, is the human cytoplasmic NADP-specific enzyme. Its subcellular localization was shown to be in both peroxisomes and the cytoplasm.

Immunogen

peptide corresponding to mutation R132H of human IDH1.

Application

Anti-IDH1 (R132H) antibody has been used:
  • in immunoblotting
  • in immunohistochemistry
  • in western blotting
  • in cell cycle analysis and apoptosis assays
  • in chromatin immunoprecipitation (ChIP) assay
  • in in vitro migration assay

Biochem/physiol Actions

Isocitrate dehydrogenase 1 (IDH1) catalyzes the oxidative decarboxylation of isocitrate into α α -KG) using NADP as co-substrate. Mutations in IDH1 are specific to Arg132 (R132) and endow them with the function of generating 2-hydroxyglutarate (2HG) instead of α-KG. This product alters gene transcription through effects on DNA and histone methylation. Several IDH1 mutations exist, including R132H, R132C, R132S, R132G and R132L. Each may result in different tumor type with varied malignant progression. The most frequent known mutation (>90%) is the alteration of arginine to histidine (R132H). Hence, antibodies that recognize the IDH1R132H mutation can be useful for the diagnosis of mutation-bearing tumors like gliomas.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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

10 - Combustible liquids

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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Bin Sheng Wong et al.
Nature biomedical engineering, 5(1), 26-40 (2020-09-30)
Clinical scores, molecular markers and cellular phenotypes have been used to predict the clinical outcomes of patients with glioblastoma. However, their clinical use has been hampered by confounders such as patient co-morbidities, by the tumoral heterogeneity of molecular and cellular
Peroxisomal localization and function of NADP+-specific isocitrate dehydrogenases in yeast
Lu Q and McAlister-H L.
Archives of Biochemistry and Biophysics, 493(2), 125-134 (2010)
IDH1R132H decreases the proliferation of U87 glioma cells through upregulation of microRNA-128a
Nie Q M, et al.
Molecular Medicine Reports, 12(5), 6695-6701 (2015)
Expression of Idh1R132H in the murine subventricular zone stem cell niche recapitulates features of early gliomagenesis
Bardella C, et al.
Cancer Cell, 30(4), 578-594 (2016)
Yongying Gao et al.
Molecular medicine reports, 23(5) (2021-03-25)
Isocitrate dehydrogenase1 (IDH1) mutation is the most important genetic change in glioma. The most common IDH1 mutation results in the amino acid substitution of arginine 132 (Arg/R132), which is located at the active site of the enzyme. IDH1 Arg132His (R132H)

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