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Merck
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Documentos Principais

SAB4200592

Sigma-Aldrich

Anti-IDH1 antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Sinônimo(s):

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

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About This Item

Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

rabbit

conjugado

unconjugated

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

Formulário

buffered aqueous solution

reatividade de espécies

mouse, human

concentração

~1.0 mg/mL

técnica(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.

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... IDH1(3417)

Descrição geral

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

Imunogênio

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).

Ações bioquímicas/fisiológicas

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.

forma física

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

Exoneração de responsabilidade

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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Código de classe de armazenamento

10 - Combustible liquids

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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Cancer-associated Isocitrate Dehydrogenase Mutations Inactivate NADPH-dependent Reductive Carboxylation
Leonardi R, et al.
The Journal of Biological Chemistry, 287, 14615-14620 (2012)
Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1alpha
Zhao S, et al.
Science, 324, 261-265 (2009)
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)
Altered cancer cell metabolism in gliomas with mutant IDH1 or IDH2
Borodovsky A, et al.
Current Opinion in Oncology, 24, 83-83 (2012)
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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