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SAB4200592

Sigma-Aldrich

Anti-IDH1 antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Synonyme(s) :

Anti-IDH, Anti-IDP, Anti-PICD, Anti-isocitrate dehydrogenase 1 (NADP+), Anti-soluble

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Espèces réactives

mouse, human

Concentration

~1.0 mg/mL

Technique(s)

immunoblotting: 1-2 μg/mL using extracts of mouse brain (S1 fraction).
immunoprecipitation (IP): 10 μg using lysates of HepG2 cells.
indirect immunofluorescence: 2-4 μg/mL using U-87 glioblastoma cells.

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... IDH1(3417)

Catégories apparentées

Description générale

Isocitrate dehydrogenase 1 (IDH1) is an isoform of IDH enzyme. It is a cytoplasmic NADP+-dependent enzyme, localized both in the cytoplasm and peroxisomes.

Immunogène

synthetic peptide corresponding to an internal sequence of human IDH1, conjugated to KLH. The corresponding sequence is highly conserved in mouse (single amino acid substitution) and highly conserved in rat IDH1 (89% sequence identity).

Actions biochimiques/physiologiques

Isocitrate dehydrogenase (IDH) is a key metabolic enzyme that catalyzes the oxidative decarboxylation of isocitrate into α-ketoglutarate (αKG) in the cytosol, by using either NAD+ or NADP+ as co-substrates. IDH1 appears to have a tumor suppressor activity and its inactivation leads to tumorigenesis partially mediated by induction of the HIF1 pathway. A genome-wide mutation study has shown that IDH1 is mutated in glioblastoma, acute myeloid leukemia (AML) and chondrosarcoma. Mutations in IDH1 specific to Arg132 (R132) impart the enzyme′s ability to generate 2- hydroxyglutarate (2HG) instead of αKG. Several IDH1 mutations have been identified in gliomas, including R132H, R132C, R132S, R132G and R132L, each may result in different tumor type with varied malignant progression.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

IDH1 and IDH2 mutations are frequent events in central chondrosarcoma and central and periosteal chondromas but not in other mesenchymal tumours
Amary MF, et al.
The Journal of Pathology, 224, 334-343 (2011)
Cancer-associated Isocitrate Dehydrogenase Mutations Inactivate NADPH-dependent Reductive Carboxylation
Leonardi R, et al.
The Journal of Biological Chemistry, 287, 14615-14620 (2012)
Altered cancer cell metabolism in gliomas with mutant IDH1 or IDH2
Borodovsky A, et al.
Current Opinion in Oncology, 24, 83-83 (2012)
Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1alpha
Zhao S, et al.
Science, 324, 261-265 (2009)
Lenny Dang et al.
Nature, 462(7274), 739-744 (2009-11-26)
Mutations in the enzyme cytosolic isocitrate dehydrogenase 1 (IDH1) are a common feature of a major subset of primary human brain cancers. These mutations occur at a single amino acid residue of the IDH1 active site, resulting in loss of

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