Mitochondrial membrane ATP synthase (F(1)F(0) 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, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) 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.

ATP synthase alpha chain, mitochondrial; ATP synthase subunit alpha; ATP synthase subunit alpha mitochondrial; ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle; ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, 1; ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, isoform 1, cardiac muscle; ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit, isoform 2, non-cardiac muscle-like 2; ATP sythase (F1 ATPase) alpha subunit; ATP5A; Atp5a1; ATP5AL2; ATPA_HUMAN; ATPM; Epididymis secretory sperm binding protein Li 123m; hATP1; HEL-S-123m; MC5DN4; mitochondrial; Mitochondrial ATP synthetase; Mitochondrial ATP synthetase oligomycin resistant; Modifier of Min 2 mouse homolog; Modifier of Min 2, mouse, homolog of; MOM2; OMR; ORM; OTTHUMP00000163475;

F1MLB8, P25705

60kDa

Mouse monoclonal

Cow, Human, Mouse, Rat

WB 1:500-1:2000, IP 1:50-100

Store at -20 °C. Stable for 12 months from date of receipt.