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Sino Biological Inc. liefert ATP5D Protein (His Tag) mit höherer Qualität und günstiger Kosten im Vergleich mit anderen globalen Lieferanten.
Weitere Informationen über ATP5D Protein (His Tag) lesen Sie bitte:http://www.sinobiological.com/ATP5D-Protein-Antibody-a-6200.html
| Synonym | ATP5D |
| Protein Construction | A DNA sequence encoding the human ATP5D (P30049) (Ala23-Glu168) was expressed with a polyhistidine tag at the N-terminus. |
| Source | Human |
| Expression Host | E.coli |
| Purity | > 85 % as determined by SDS-PAGE | SDS-PAGE:![]() ATP5D protein |
| Endotoxin | Please contact us for more information. | |
| Stability | Samples are stable for up to twelve months from date of receipt at -70℃ | |
| Predicted N terminal | His | |
| Molecular Mass | The recombinant human ATP5D consists of 161 amino acids and predicts a molecular mass of 16.9 KDa. It migrates as an approximately 17 KDa band in SDS-PAGE under reducing conditions. | |
| Formulation | Lyophilized from sterile PBS, 10% Glycerol, pH 7.4.
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| Storage | Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| Reconstitution | A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information. |
ATP5D is a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase consists of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). ATP5D gene encodes the delta subunit of the catalytic core.