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Merck
CN

SAB4200547

Anti-IDH1 (R132S) antibody, Mouse monoclonal

clone SMab-1, purified from hybridoma cell culture

别名:

Monoclonal Anti-IDCD, Monoclonal Anti-IDH, Monoclonal Anti-IDH1 (R132S) antibody produced in mouse, Monoclonal Anti-IDP, Monoclonal Anti-IDPC, Monoclonal Anti-NADP(+)-specific ICDH, Monoclonal Anti-NADP-dependent isocitrate dehydrogenase, cytosolic, Monoclonal Anti-Oxalosuccinate decarboxylase, Monoclonal Anti-PICD, Monoclonal Anti-isocitrate dehydrogenase 1 (NADP+), soluble, NADP-dependent isocitrate dehydrogenase, peroxisomal

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关于此项目

NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
SMab-1, monoclonal
Application:
—
Citations:
4

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biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

SMab-1, monoclonal

form

buffered aqueous solution

mol wt

antigen ~43 kDa

species reactivity

human

concentration

~1 mg/mL

technique(s)

immunoblotting: 0.25-0.5 μg/mL using using total cell extracts of HEK-293T cells overexpressing IDH1R132S

UniProt accession no.

O75874

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

mutation (Arg132Ser)

Gene Information

human ... IDH1(3417)

General description

Monoclonal Anti-IDH1 (R132S) (mouse IgG1 isotype) is derived from the hybridoma SMab1 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized by a peptide. Isocitrate dehydrogenase 1 (IDH1) is a homodimeric, nicotinamide adenine dinucleotide phosphate (NADP)-specific enzyme. It is localized in the peroxisomes and cytoplasm. IDH1 is mapped on the human chromosome at 2q34.

Immunogen

immunized a peptide corresponding to the mutation R132S of human IDH1. The isotype is determined by ELISA using Mouse Monoclonal Antibody Isotyping Reagents (Sigma ISO-2).

Application

Monoclonal Anti-IDH1 (R132S) antibody produced in mouse may be used in:
  • immunoblotting
  • immunofluorescence
  • immunohistochemistry

Biochem/physiol Actions

Isocitrate dehydrogenase (IDH) plays an important role in catalyzing the oxidative decarboxylation of isocitrate to α-ketoglutarate (αKG). Mutations in this gene are associated with several cancers, such as glioblastoma, acute myeloid leukemia (AML) and chondrosarcoma. Mutation in IDH1 specific to Arg132 results in the formation of 2-hydroxyglutarate (2HG) instead of αKG. 2HG hinders DNA and histone methylation resulting in alteration of gene transcription.
Monoclonal Anti- IDH1 (R132S) recognizes only human R132S mutated IDH1 and does not cross react with others.

Physical form

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

Preparation Note

For extended storage, freeze at -20 °C in working aliquots. Repeated freezing and thawing,or storage in “frost-free” freezers,is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

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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存储类别

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

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历史批次信息供参考:

分析证书(COA)

Lot/Batch Number
112M4869
112M4869V

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Screen for IDH1, IDH2, IDH3, D2HGDH and L2HGDH mutations in glioblastoma
Krell D, et al.
PLoS ONE, 6(5), e19868-e19868 (2011)
Altered cancer cell metabolism in gliomas with mutant IDH1 or IDH2
Borodovsky A, et al.
Current Opinion in Oncology, 24(1), 83-83 (2012)
Molecular pathogenesis of IDH mutations in gliomas
Ichimura Koichi
Brain Tumor Pathology, 29(3), 131-139 (2012)
IDH mutation impairs histone demethylation and results in a block to cell differentiation
Lu C, et al.
Nature, 483(7390), 474-478 (2012)

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