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リコンビナント
expressed in E. coli
アッセイ
≥95% (SDS-PAGE)
フォーム
aqueous solution
比活性
≥1000 units/mg protein
UniProtアクセッション番号
輸送温度
wet ice
保管温度
−20°C
詳細
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:
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.
単位の定義
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.
調製ノート
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.
法的情報
Trizma is a registered trademark of Merck KGaA, Darmstadt, Germany
保管分類コード
10 - Combustible liquids
WGK
WGK 2
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
SAE0097-BULK:
SAE0097-50UG-PW:
SAE0097-VAR:
SAE0097-50UG:
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試験成績書（COA）
Lot/Batch Number
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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
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
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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