Recombinant Human ATP5F1C
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Product specifications
| Category | Proteins and Peptides |
| Host | E.Coli |
| Reactivity | Human |
| Assay Data | Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg/ml by gently pipetting 2-3 times, don't vortex. |
| Recommended Dilution | ¥ |
| Isotype | ¥ |
| Clone ID | ¥ |
| Observed MW | 35.1 kDa |
| Expression | 156-284 |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| Size 1 | 50μg |
| Size 2 | 200μg |
| Size 3 | 1mg |
| Form | Lyophilized powder |
| Tested Applications | Western Blot, ELISA |
| Buffer | Lyophilized from a 0.2 μm filtered solution in 10 mM Hepes, 500 mM NaCl with 5% trehalose, pH 7.4. |
| Availability | 7 days |
| Storage | The lyophilized protein is stable at -20 °C for up to 1 year. After reconstitution, the protein solution is stable at -20 to -80 °C for 3 months or 1 week at 2 to 8 °C under sterile conditions. For extended storage, it is recommended to further dilute in working aliquots, avoid repeated freeze/thaw cycle. |
| UniProt ID | P36542 |
| Alias | ATP synthase subunit gamma, mitochondrial, ATP synthase F1 subunit gamma, F-ATPase gamma subunit |
| Background | Protein ATP5F1C |
| Status | RUO |
| Note | Tag : N-terminal His-IF2DI Tag |
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ATP5F1C antibody
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. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). 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.
Ver ProductoATP5F1C antibody
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. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). 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.
Ver Producto