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重組細胞
expressed in E. coli
化驗
≥95% (SDS-PAGE)
形狀
aqueous solution
比活性
≥1000 units/mg protein
UniProt登錄號
運輸包裝
wet ice
儲存溫度
−20°C
一般說明
D-2-羟基戊二酸脱氢酶(D2HGDH)是D-2-羟基酸NAD+依赖性脱氢酶家族的成员。D2HGDH催化α-酮戊二酸(α-KG)转化为D-2-羟基戊二酸(D2HG),并与NADH氧化为NAD+偶联。
已经报道了来自发酵酸氨基球菌的D2HGDH的晶体结构。来自发酵酸氨基球菌的D2HGDH已用于几种酶促测定,例如:
已经报道了来自发酵酸氨基球菌的D2HGDH的晶体结构。来自发酵酸氨基球菌的D2HGDH已用于几种酶促测定,例如:
- 基于酮化合物和L-谷氨酸的转氨作用,测量氨基转移酶活性的连续分光光度测定法,其产生相应的氨基化合物和2-氧代戊二酸酯。
- 测定生物体液(例如血清,尿液,细胞培养上清液以及细胞或组织裂解液)中的D2HG水平。
- 用于测量支链氨基酸氨基转移酶活性的偶联测定系统。
單位定義
一个单位的酶将1μmole NADH氧化为NAD+,并在37℃,pH 8.0下每分钟将α-酮戊二酸还原为(D)-2-羟基戊二酸。
準備報告
该重组D2HGDH产品以水溶液的形式提供在20 mM Trizma®缓冲液(pH 7.5)中,包含150 mM NaCl和10%甘油。
法律資訊
T3P is a registered trademark of Archimica GmbH
儲存類別代碼
10 - Combustible liquids
水污染物質分類(WGK)
WGK 2
閃點(°F)
Not applicable
閃點(°C)
Not applicable
其他客户在看
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
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
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.
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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