ATP5F1A antibody - 100 µg
Host : Mouse
Clonality: Monoclonal
Clone: 9G0
Isotype: IgG1
Immunogen: ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle
Purity: ≥95% as determined by SDS-PAGE
Form: Liquid
Molecular weight: 50-55 kDa
Uniprot: P25705
Gene id: 498
Background: 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).
Field of research: Metabolism
Storage conditions: PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20°C for 12 months(Avoid repeated freeze
thaw cycles.)
Applications: ELISA, IHC, IF, WB, FC
Dilution: WB: 1:500-1:2000; IP: 1:500-1:1000; IHC: 1:20-1:200; IF: 1:20-1:200
Target: ATP5F1A
Purification: Protein A+G purification
Reactivity: Human, Mouse, Rat
![]()
Clonality: Monoclonal
Clone: 9G0
Isotype: IgG1
Immunogen: ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle
Purity: ≥95% as determined by SDS-PAGE
Form: Liquid
Molecular weight: 50-55 kDa
Uniprot: P25705
Gene id: 498
Background: 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).
Field of research: Metabolism
Storage conditions: PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20°C for 12 months(Avoid repeated freeze
thaw cycles.)
Applications: ELISA, IHC, IF, WB, FC
Dilution: WB: 1:500-1:2000; IP: 1:500-1:1000; IHC: 1:20-1:200; IF: 1:20-1:200
Target: ATP5F1A
Purification: Protein A+G purification
Reactivity: Human, Mouse, Rat