

| Número de catálogo | HD823012 |
|---|---|
| Descripción |
Recombinant Human MT-ATP6 Protein, N-GST & C-His (HD823012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
|
| Sistema de expresión | E. coli |
| Número de acceso | P00846 |
| Longitud de proteína | Phe26-Trp68&Phe117-Ile138&Ile209-Thr226 |
| Aplicaciones | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Especies | Homo sapiens (Human) |
| Naturaleza | Recombinant |
| Nivel de endotoxinas | Please contact with the lab for this information. |
| Pureza | >90% as determined by SDS-PAGE. |
| Forma | Lyophilized |
| Buffer de almacenamiento | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Consulte la información específica del buffer en la copia impresa del datasheet o en el COA específico del lote. |
| Reconstitución | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Envío | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Estabilidad y almacenamiento | 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. |
| Nombres alternativos | ATP synthase F(0) complex subunit a, ATP6, ATPASE6, F-ATPase protein 6, MT-ATP6, MTATP6, Proton-conducting channel, ATP synthase F(0) complex subunit a |
| Fondo | ATP synthase F(0) complex subunit a is a ~24 kDa protein. Subunit a, 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 (Probable). 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). With the subunit c (ATP5MC1), forms the proton-conducting channel in the F(0) domain, that contains two crucial half-channels (inlet and outlet) that facilitate proton movement from the mitochondrial intermembrane space (IMS) into the matrix. 1. Lai, Y. et al. (2023) Molecular cell 83, 2137-2147.e4. PMID: 37244256 |
| Nota | For research use only |
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