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Documentos Principais

SAE0097

Sigma-Aldrich

D-2-Hydroxyglutarate Dehydrogenase (D2HGDH) from Acidaminococcus fermentans

recombinant, expressed in E. coli, aqueous solution

Sinônimo(s):

D2HGDH, HGDH, L-2-hydroxyglutarate dehydrogenase

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About This Item

Número da licença da enzima:
1.1. 99.2
Código UNSPSC:
12352202
NACRES:
NA.54

recombinante

expressed in E. coli

Ensaio

≥95% (SDS-PAGE)

Formulário

aqueous solution

atividade específica

≥1000 units/mg protein

nº de adesão UniProt

Condições de expedição

wet ice

temperatura de armazenamento

−20°C

Descrição geral

D-2-Hydroxyglutarate Dehydrogenase (D2HGDH) is a member of the D-2-hydroxyacid NAD+ dependent dehydrogenase family of proteins. D2HGDH catalyzes the conversion of α-ketoglutarate (α--KG) to D-2-hydroxyglutarate (D2HG), coupled to the oxidation of NADH to NAD+ .

The crystal structure of D2HGDH from Acidaminococcus fermentans has been reported. D2HGDH from Acidaminococcus fermentans has been used in several enzymatic assays, such as:
  • A continuous spectrophotometric assay to measure the activity of aminotransferases, based on the transamination of a keto compound and L-glutamate, which yields a corresponding amino compound and 2-oxoglutarate.
  • Determination of D2HG levels in biological fluids such as serum, urine, cell culture supernatants, and cell or tissue lysates.
  • A coupled assay system to measure branched-chain amino acid aminotransferase activity.

Definição da unidade

One unit of enzyme oxidizes 1 μmole of NADH to NAD+ coupled to the reduction of α-ketoglutarate to (D)-2-hydroxyglutarate per minute at 37°C at pH 8.0.

Nota de preparo

This recombinant D2HGDH product is supplied as an aqueous solution in 20 mM Trizma® buffer, pH 7.5, with 150 mM NaCl, and 10% glycerol.

Informações legais

Trizma is a registered trademark of Merck KGaA, Darmstadt, Germany

Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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Berta M Martins et al.
The FEBS journal, 272(1), 269-281 (2005-01-07)
NAD(+)-dependent (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyses the reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate and belongs to the d-2-hydroxyacid NAD(+)-dependent dehydrogenase (d-2-hydroxyacid dehydrogenase) protein family. Its crystal structure was determined by phase combination to 1.98 A resolution. Structure-function relationships obtained by the comparison
Xuejing Yu et al.
Analytical biochemistry, 431(2), 127-131 (2012-09-25)
A continuous general spectrophotometric assay for measuring the activity of aminotransferases has been developed. It is based on the transamination of a keto compound (amino acceptor) and l-glutamate (amino donor), yielding the corresponding amino compound and 2-oxoglutarate. The rate of
Jörg Balss et al.
Acta neuropathologica, 124(6), 883-891 (2012-11-03)
Levels of (D)-2-hydroxyglutarate [D2HG, (R)-2-hydroxyglutarate] are increased in some metabolic diseases and in neoplasms with mutations in the isocitrate dehydrogenase 1 (IDH1) and isocitrate dehydrogenase 2 (IDH2) genes. Determination of D2HG is of relevance to diagnosis and monitoring of disease.
Xuejing Yu et al.
The FEBS journal, 281(1), 391-400 (2013-11-12)
Branched-chain amino acid aminotransferase (BCAT) plays a key role in the biosynthesis of hydrophobic amino acids (such as leucine, isoleucine and valine), and its substrate spectrum has not been fully explored or exploited owing to the inescapable restrictions of previous

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