The Mouse (COX4I1) Cytochrome Coxidase Subunit 4 Isoform 1, Mitochondrial ELISA Kit measures Cytochrome c oxidase subunit 4 isoform 1, mitochondrial in Mouse samples. The plate has been pre-coated with Mouse COX4I1 antibody. COX4I1 present in the sample is added and binds to antibodies coated on the wells. And then biotinylated Mouse COX4I1 Antibody is added and binds to COX4I1 in the sample. Then Streptavidin-HRP is added and binds to the Biotinylated COX4I1 antibody. After incubation unbound Streptavidin-HRP is washed away during a washing step. Substrate solution is then added and color develops in proportion to the amount of Mouse COX4I1. The reaction is terminated by addition of acidic stop solution and absorbance is measured at 450 nm.
BackgroundComponent 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 subunbit 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: UniProt Consortium (2025)
Shipping ConditionShipped on cold gel packs.
Storage Condition and Shelf Life
2-8C
AnalyteCytochrome c oxidase subunit 4 isoform 1, mitochondrial
