ATP5F1D antibody - 100 µg
Host : Rabbit
Clonality: Polyclonal
Clone:
Isotype: IgG
Immunogen: ATP synthase, H+ transporting, mitochondrial F1 complex, delta subunit
Purity: ≥95% as determined by SDS-PAGE
Form: Liquid
Molecular weight: 15-17 kDa
Uniprot: P30049
Gene id: 513
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 turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. 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.
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, WB, IHC
Dilution: WB: 1:500-1:2000; IHC: 1:20-1:200
Target: ATP5F1D
Purification: Immunogen affinity purified
Reactivity: Human, Mouse, Rat
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Clonality: Polyclonal
Clone:
Isotype: IgG
Immunogen: ATP synthase, H+ transporting, mitochondrial F1 complex, delta subunit
Purity: ≥95% as determined by SDS-PAGE
Form: Liquid
Molecular weight: 15-17 kDa
Uniprot: P30049
Gene id: 513
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 turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. 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.
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, WB, IHC
Dilution: WB: 1:500-1:2000; IHC: 1:20-1:200
Target: ATP5F1D
Purification: Immunogen affinity purified
Reactivity: Human, Mouse, Rat