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Merck

SAB4200592

Sigma-Aldrich

Anti-IDH1 antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Synonym(e):

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

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About This Item

UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

rabbit

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Speziesreaktivität

mouse, human

Konzentration

~1.0 mg/mL

Methode(n)

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.

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... IDH1(3417)

Verwandte Kategorien

Allgemeine Beschreibung

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

Immunogen

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).

Biochem./physiol. Wirkung

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.

Physikalische Form

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

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

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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