Cytochrome C oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. It is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane. The complex consists of 13 mitochondrial- and nuclear-encoded subunits. The mitochondrially-encoded subunits perform the electron transfer and proton pumping activities. The functions of the nuclear-encoded subunits are unknown but they may play a role in the regulation and assembly of the complex. This gene encodes the nuclear-encoded subunit Vb of the human mitochondrial respiratory chain enzyme.

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Flow cytometric analysis of COX5B expression in H9c2 cells using COX5B antibody . Green, isotype control; red, COX5B.

Immunocytochemical staining of H9C2 cells with COX5B antibody . Nuclei were stained blue with DAPI; COX5B was stained magenta with Alexa Fluor® 647. Images were taken using Leica stellaris 5. Protein abundance based on laser Intensity and smart gain: Medium. Scale bar, 20 μm.

Western blotting analysis using COX5B antibody . Total cell lysates (30 μg) from various cell lines were loaded and separated by SDS-PAGE. The blot was incubated with COX5B antibody and HRP-conjugated goat anti-rabbit secondary antibody respectively. Image was developed using NaQ™ ECL Substrate Kit .

Western blotting analysis using COX5B antibody . COX5B expression in wild-type (WT) and COX5B shRNA knockdown (KD) HeLa cells with 20 μg of total cell lysates. Hsp90 α serves as a loading control. The blot was incubated with COX5B antibody and HRP-conjugated goat anti-rabbit secondary antibody respectively. Image was developed using FeQ™ ECL Substrate Kit .

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