Invitrogen™ MTCO2 Monoclonal Antibody (12C4F12)

Description

To facilitate the study of COX structure and mitochondrial biogenesis, Invitrogen offers several subunit-specific mouse anti-OxPhos Complex IV monoclonal antibodies. The binding specificity of our anti-OxPhos Complex IV monoclonal antibody preparations allows researchers to investigate the regulation, assembly, and orientation of COX subunits in a variety of organisms. The antibodies have also proven valuable for analyzing human mitochondrial myopathies and related disorders as well as mitochondrial DNA depletion due to drug toxicity. Alexa Fluor TM 488 and Alexa Fluor TM 594 conjugates of anti- OxPhos Complex IV subunit I are also available for direct staining of these COX proteins. Cell lines can be screened for subunit expression levels for each of the OxPhos complexes by simple western blotting. These results can be combined with native gel electrophoresis or sucrose gradient centrifugation to gather additional information regarding the assembly state of the OxPhos complexes. Many of our antibodies against OxPhos subunits may also be used for immunocytochemical analysis. Image analysis of an antibody's staining pattern can reveal the relative expression and localization of a subunit. This approach has been particularly useful for studying OxPhos subunit expression in diseased muscle fibers and for screening Complex IV-deficient patients. The antibody was produced in vitro using hybridomas grown in serum-free medium, and then purified by biochemical fractionation. Near ...

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. [UniProt].