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Human MT-CO1 (Cytochrome Coxidase Subunit 1) ELISA Kit

Human MT-CO1 (Cytochrome Coxidase Subunit 1) ELISA Kit

The Human (MT-CO1) Cytochrome Coxidase Subunit 1 ELISA Kit measures Cytochrome c oxidase subunit 1 in samples. The plate has been pre-coated with Human MT-CO1 antibody. MT- CO1 present in the sample is added and binds to antibodies coated on the wells. And then biotinylated Human MT-CO1 Antibody is added and binds to MT-CO1 in the sample. Then Streptavidin-HRP is added and binds to the Biotinylated MT-CO1 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 Human MT-CO1. The reaction is terminated by addition of acidic stop solution and absorbance is measured at 450 nm.

Catalog No: E5154Hu
Regular price $595.00 USD
Regular price $458.00 USD Sale price $595.00 USD
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2.5 weeks
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Product Details

Species Reactivity Human
Sensitivity 7.25 ng/L
Detection Range 15-3000 ng/L
Sample Type Serum, plasma, cell culture supernates
Incubation(s) 1.5 hour(s)
Research Areas Tags & Cell Markers
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: UniProt Consortium (2025)
Shipping Condition Shipped on cold gel packs.
Storage Condition and Shelf Life 2-8C
Analyte Cytochrome c oxidase subunit 1
Regulatory Status For Research Use Only
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