RM5175

ATP5A1 (11Q15) Rabbit Monoclonal Antibody

Atp5a1; ATP5AL2; ATPM; hATP1; HEL-S-123m; MC5DN4; MOM2;

Affinity-chromatography

常规抗体

ATP5F1A

WB

Human,Mouse,Rat

Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% New type preservative N and 50% glycerol. Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle.

498

P25705

WB 1:500~1:2000 IHC 1:50~1:200 ICC/IF 1:50~1:200 FC 1:50

60kDa

Rabbit IgG

ATP5A1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.

Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord

Mitochondrion. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P19483}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19483}; Matrix side {ECO:0000250|UniProtKB:P19483}. Cell membrane; Peripheral membrane protein; Extracellular side. Note=Colocalizes with HRG on the cell surface of T-cells (PubMed:19285951).

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 (PubMed:30146159).

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