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ATP5C1 Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
  • WB - ATP5C1 Antibody AP53285
    All lanes : Anti-ATP5C1 Antibody at 1:1000 dilution Lane 1: human heart lysate Lane 2: HepG2 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L),Peroxidase conjugated at 1/10000 dilution. Predicted band size : 33 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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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
Primary Accession P36542
Reactivity Human
Host Rabbit
Clonality Polyclonal
Calculated MW 33 KDa
Antigen Region 130-179 aa
Additional Information
Gene ID 509
Other Names ATP synthase subunit gamma, mitochondrial, F-ATPase gamma subunit, ATP5C1, ATP5C, ATP5CL1
Dilution WB~~ 1:1000
Format Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.09% (W/V) sodium azide and 50% glycerol
StorageStore at -20 °C.Stable for 12 months from date of receipt
Protein Information
Name ATP5F1C (HGNC:833)
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. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). 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.
Cellular Location Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05631}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05631}; Matrix side {ECO:0000250|UniProtKB:P05631}
Tissue Location Isoform Heart is expressed specifically in the heart and skeletal muscle, which require rapid energy supply. Isoform Liver is expressed in the brain, liver and kidney. Isoform Heart and Isoform Liver are expressed in the skin, intestine, stomach and aorta
Research Areas
Citations (0)
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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. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). 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.

References

Matsuda C.,et al.J. Biol. Chem. 268:24950-24958(1993).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Ebert L.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
Deloukas P.,et al.Nature 429:375-381(2004).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

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$ 350.00
Cat# AP53285
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