

| Numéro de catalogue | HY325022 |
|---|---|
| Description |
Recombinant Human MT-ATP8 Protein, N-GST & C-His (HY325022) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
|
| Système d'expression | E. coli |
| Numéro d'accès | P03928 |
| Longueur de protéine | Lys27-Ser68 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Espèces | Homo sapiens (Human) |
| Nature | Recombinant |
| Niveau d'endotoxines | Please contact with the lab for this information. |
| Pureté | >90% as determined by SDS-PAGE. |
| Forme | Lyophilized |
| Tampon de stockage | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Reférez-vous aux informations spécifiques sur le tampon dans la copie papier du datasheet ou dans le COA spécifique au lot. |
| 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. |
| Expédition | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Stabilité et stockage | 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. |
| Noms alternatifs | A6L, ATP synthase F(0) complex subunit 8, ATP8, ATPASE8, F-ATPase subunit 8, MT-ATP8, MTATP8 |
| Contexte | ATP synthase F(0) complex subunit 8 is a ~7 kDa protein. Subunit 8, 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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