Human COX5A, C-His Tag Protein
cat.: HA210534
| Product name: |
Human COX5A, C-His Tag |
| Catalog No.: |
HA210534 |
| Bio-Activity: |
Testing in progress. |
| Purity: |
>90% as determined by SDS-PAGE. |
| Endotoxin: |
Less than 1.0 EU per μg by the LAL method. |
| Formulation: |
Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4, 5% Trehalose, 5% mannitol. |
| Background: |
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. |
| Source: |
E.coli |
| Storage: |
Please avoid repeated freeze-thaw cycles. Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃ It is recommended that aliquot the reconstituted solution to minimize freeze-thaw cycles. |
| Reconstitution: |
Reconstitute at 250 μg/ml in sterile water. |