COX5B Rabbit mAb
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND

Application
| WB, IHC-P, IHC-F, IP, ICC |
|---|---|
| Primary Accession | P10606 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Monoclonal Antibody |
| Calculated MW | 13696 Da |
| Gene ID | 1329 |
|---|---|
| Other Names | COX5B |
| Dilution | WB~~1/500-1/1000 IHC-P~~N/A IHC-F~~N/A IP~~N/A ICC~~N/A |
| Format | 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40%Glycerol, 0.01% sodium azide and 0.05% BSA. |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Name | COX5B |
|---|---|
| Function | 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. |
| Cellular Location | Mitochondrion inner membrane; Peripheral membrane protein; Matrix side |

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