ATP5A Polyclonal Antibody dm-16383

Catalog No dm-16383 

Isotype IgG 

Reactivity Human;Mouse;Rat 

Applications WB;IHC;IF;ELISA 

Gene Name ATP5A1 

Protein Name ATP synthase subunit alpha mitochondrial 

Immunogen The antiserum was produced against synthesized peptide derived from human ATP5A1. AA range:201-250 

Specificity ATP5A Polyclonal Antibody detects endogenous levels of ATP5A protein. 

Formulation Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide. 

Source Polyclonal, Rabbit,IgG 

Purification The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen. 

Dilution WB: 1/500 - 1/2000. IHC: 1/100 - 1/300. ELISA: 1/40000.. IF 1:50-200

Concentration 1 mg/ml 

Purity ≥90% 

Storage Stability -20°C/1 year

Synonyms ATP5A1; ATP5A; ATP5AL2; ATPM; ATP synthase subunit alpha; mitochondrial 

Observed Band 60kD 

Cell Pathway Mitochondrion . Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side . Cell membrane ; Peripheral membrane protein ; Extracellular side . Colocalizes with HRG on the cell surface of T-cells (PubMed:19285951). . 

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

Function 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.,