Products

ATP5A1 antibody

Synonyms:ATP5A antibody, ATP5AL2 antibody, ATPM antibody
Catalogue No.:FNab00703Reativity:Human, Mouse, Rat
Host:MouseTested Application:ELISA, IHC, IF, WB, FC
Clonality:monoclonalIsotype:IgG1
  • SPECIFICATIONS
Product Name
ATP5A1 antibody
Catalogue No.
FNab00703
Size
100μg
Form
liquid
Purification
Protein A+G purification
Purity
≥95% as determined by SDS-PAGE
Clonality
monoclonal
Isotype
IgG1
Clone ID
9G0
Storage
PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.)
Immunogen
Immunogen
ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle
Alternative Names
ATP5A antibody, ATP5AL2 antibody, ATPM antibody
UniProt ID
P25705
Observed MW
50-55 kDa
Application
Tested Applications
ELISA, IHC, IF, WB, FC
Recommended dilution
WB: 1:500-1:2000; IP: 1:500-1:1000; IHC: 1:20-1:200; IF: 1:20-1:200
Validated Images
Various lysates were subjected to SDS PAGE followed by western blot with FNab00703(ATP5A1 antibody) at dilution of 1:1000
IP Result of anti-ATP5A1 (IP: FNab00703, 5ug; Detection: FNab00703 1:500) with mouse heart tissue lysate 4000ug.
Immunohistochemistry of paraffin-embedded human liver using FNab00703(ATP5A1 antibody) at dilution of 1:50
Immunofluorescent analysis of Hela cells using FNab00703 (ATP5A1 antibody) at dilution of 1:25
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).