Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) 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. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
规格 | 价格/CNY | 货期 | 数量 | |
---|---|---|---|---|
20 μg | ¥ 1,800 | 20日内发货 | ||
100 μg | ¥ 3,420 | 20日内发货 | ||
1 mg | ¥ 14,600 | 20日内发货 |
产品描述 | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) 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. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. |
种属 | Mouse |
表达系统 | E. coli |
标签 | N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged |
蛋白编号 | P56480 |
别名 | ATP synthase F1 subunit beta, Atp5b, Atp5f1b, ATP synthase subunit beta, mitochondrial |
氨基酸序列 | YSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGNEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHGS Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request. |
蛋白构建 | 230-529 aa |
蛋白纯度 | > 85% as determined by SDS-PAGE. |
分子量 | 52.8 kDa (predicted) |
缓冲液 | Tris-based buffer,50% glycerol |
复溶方法 | A hardcopy of COA with reconstitution instructions is sent along with the products. Please refer to it for detailed information. |
存储 |
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C. |
运输方式 |
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. |
研究背景 | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) 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. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. |
bottom
您可能有的问题的答案可以在重组蛋白操作手册中找到
ATP5B Protein, Mouse, Recombinant (His & Myc & SUMO) ATP synthase F1 subunit beta Atp5b Atp5f1b ATP synthase subunit beta, mitochondrial recombinant recombinant-proteins proteins protein