The Porcine (ATP5A1) Atp Synthase Subunit Alpha, Mitochondrial ELISA Kit measures ATP Synthase subunit alpha, mitochondrial in Porcine samples. The plate has been pre-coated with Porcine ATP5A1 antibody. ATP5A1 present in the sample is added and binds to antibodies coated on the wells. And then biotinylated Porcine ATP5A1 Antibody is added and binds to ATP5A1 in the sample. Then Streptavidin-HRP is added and binds to the Biotinylated ATP5A1 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 Porcine ATP5A1. The reaction is terminated by addition of acidic stop solution and absorbance is measured at 450 nm.
Research AreasTags and Cell Markers, Signal Transduction, Metabolism
BackgroundMitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity). Source: UniProt Consortium (2025)
