重组人 PDHB 蛋白 (GST tag N-Terminus)
Recombinant Human PDHB protein (GST tag N-Terminus)
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Recombinant Human PDHB protein (GST tag N-Terminus) is a Human Fragment protein, in the 250 to 359 aa range, expressed in Wheat germ, suitable for ELISA, WB.
查看别名
PHE1B, PDHB, PDHE1-B
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human PDHB protein (GST tag N-Terminus) (AB152601)
ab152601 on a 12.5% SDS-PAGE stained with Coomassie Blue.
反应性数据
产品详情
序列信息
性能和储存信息
运输条件
推荐的短期储存条件
推荐的长期储存条件
分装信息
储存信息
补充信息
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
PDHB functions as an essential component of the PDC which catalyzes the decarboxylation of pyruvate linking glycolysis to the citric acid cycle. The PDC itself is a large multi-enzyme complex including other subunits such as E1 and E2 which coordinate efficiently to carry out its function. In this way PDHB contributes to energy production by enabling entry of carbon skeletons into the tricarboxylic acid cycle important for ATP generation.
Pathways
PDHB holds a significant role in central metabolic pathways namely glycolysis and the citric acid cycle. The conversion facilitated by the PDC forms a vital cornerstone for metabolic flux regulation influencing gluconeogenesis and fatty acid synthesis. PDHB also interacts with proteins such as pyruvate dehydrogenase kinase which regulates the PDC activity by phosphorylation thereby affecting energy metabolism directly.
特殊说明
形式
Liquid
常规信息
功能
Together with PDHA1 forms the heterotetrameric E1 subunit of the pyruvate dehydrogenase (PDH) complex (PubMed : 17474719, PubMed : 19081061). The PDH complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (Probable). It contains multiple copies of three enzymatic components : pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) (Probable). The E1 subunit catalyzes both the thiamine pyrophosphate (TPP)-dependent decarboxylation of pyruvate and the reductive acetylation of a lipoyl group covalently linked to the lipoyl-bearing domains of E2 (PubMed : 19081061).
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