重组人 ATP5H 蛋白 (GST tag N-Terminus)
Recombinant Human ATP5H protein (GST tag N-Terminus)
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Recombinant Human ATP5H protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 161 aa range, expressed in Wheat germ, suitable for ELISA, WB.
查看别名
ATP5H, My032, ATP5PD, ATPase subunit d, ATP synthase peripheral stalk subunit d
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human ATP5H protein (GST tag N-Terminus) (AB153084)
ab153084 on a 12.5% SDS-PAGE stained with Coomassie Blue.
反应性数据
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
ATP5H facilitates the production of ATP the energy currency of the cell. It is essential in the synthesis of ATP from ADP and inorganic phosphate driven by a proton gradient across the mitochondrial membrane. ATP5H is integral to the structure of the F1F0 ATP synthase complex ensuring efficient proton translocation and ATP synthesis. This subunit is critical for the overall function and stability of the ATP synthase complex.
Pathways
ATP5H plays a role in oxidative phosphorylation and energy metabolism pathways. This protein interacts closely with other ATP synthase subunits including ATP5B and ATP5O orchestrating the conversion of energy derived from nutrients to ATP. The oxidative phosphorylation pathway is central to energy production in eukaryotic cells and ATP5H forms an essential link in this process.
特殊说明
形式
Liquid
常规信息
功能
Subunit d, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed : 37244256). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed : 37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed : 37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (PubMed : 37244256). Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity).
序列相似性
Belongs to the ATPase d subunit family.
靶点信息
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