

| Catalog No. | HX870022 |
|---|---|
| Description |
Recombinant Human ATP5ME Protein, N-GST & C-His (HX870022) expressed in E. coli, spanning Val2-Lys69. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | E. coli |
| Accession | P56385 |
| Protein length | Val2-Lys69 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Homo sapiens (Human) |
| Nature | Recombinant |
| Endotoxin level | Please contact with the lab for this information. |
| Purity | >90% as determined by SDS-PAGE. |
| Predicted molecular weight | 35.98 kDa |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Alternate Names | ATP synthase F(0) complex subunit e, mitochondrial, ATP synthase F(0) complex subunit e, mitochondrial, N-terminally processed, ATP synthase membrane subunit e, ATP5I, ATP5K, ATP5ME, ATPase subunit e |
| Background | ATP synthase F(0) complex subunit e, mitochondrial is a ~7 kDa protein. Subunit e, 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. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary 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 (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. 1. Lai, Y. et al. (2023) Molecular cell 83, 2137-2147.e4. PMID: 37244256 |
| Note | For research use only |
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