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ATP5A1 Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - ATP5A1 Antibody AP51004
    All lanes : Anti-ATP5A1 Antibody at 1:1000 dilution Lane 1: HepG2 whole cell lysates Lane 2: H.heart tissue lysates Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L),Peroxidase conjugated at 1/10000 dilution Predicted band size : 60 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB
Primary Accession P25705
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality Polyclonal
Calculated MW 60 KDa
Additional info
Gene ID 498
Other Names ATP synthase subunit alpha, mitochondrial, ATP5A1, ATP5A, ATP5AL2, ATPM
Target/Specificity KLH conjugated synthetic peptide derived from human ATP5A1
Dilution WB~~ 1:1000
Format 0.01M PBS, pH 7.2, 0.1% Sodium azide, Glycerol 50%
StorageStore at -20 °C.Stable for 12 months from date of receipt
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

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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