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ATP5A1 / ATP Synthase Alpha Antibody (aa201-250)

Rabbit Polyclonal Antibody

     
  • WB - ATP5A1 / ATP Synthase Alpha Antibody (aa201-250) ALS14223
    Western blot of extracts from 293/RAW264.7 cells, using ATP5A1 Antibody.
    detail
  • IHC - ATP5A1 / ATP Synthase Alpha Antibody (aa201-250) ALS14223
    Anti-ATP5A1 antibody IHC of human breast.
    detail
  • IHC - ATP5A1 / ATP Synthase Alpha Antibody (aa201-250) ALS14223
    Anti-ATP5A1 antibody IHC of human heart.
    detail
  • SPECIFICATION
  • CITATIONS
  • PROTOCOLS
  • BACKGROUND
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
WB, IHC-P, E
Primary Accession P25705
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality Polyclonal
Calculated MW 60kDa
Dilution ELISA (1:40000), IHC-P (5 µg/ml), WB (1:500-1:1000)
Additional Information
Gene ID 498
Other Names ATP synthase subunit alpha, mitochondrial, ATP5A1, ATP5A, ATP5AL2, ATPM
Target/Specificity ATP5A1 Antibody detects endogenous levels of total ATP5A1 protein.
Reconstitution & Storage Short term 4°C, long term aliquot and store at -20°C, avoid freeze thaw cycles.
PrecautionsATP5A1 / ATP Synthase Alpha Antibody (aa201-250) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name ATP5F1A (HGNC:823)
Function 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).
Cellular Location 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).
Tissue Location Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord
Research Areas
Citations (0)
citation

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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).

References

Kataoka H.,et al.Biochim. Biophys. Acta 1089:393-395(1991).
Godbout R.,et al.Gene 123:195-201(1993).
Akiyama S.,et al.Biochim. Biophys. Acta 1219:129-140(1994).
Kalnine N.,et al.Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).

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$ 467.50
Cat# ALS14223
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