Anti-ATP5A1

Custom conjugation services for this antibody as available (eg. labeling of Anti-ATP5A1 with HRP. Available labels are AF: AF350, AF488, AF555, AF594, AF647, AF680, AF700, AF750. Proteins: HRP, Alkaline Phosphatase, Streptavidin. Tandems: APC, APC/Cy7, APC/AF750, APC/iFluor(TM) 700, APC/iFluor(TM) 750, PE, PE/Cy5, PE/Cy7, PE/AF610, PE/AF700, PE/iFluor(TM) 594, PE/iFluor(TM) 647, PE/iFluor(TM) 700, PE/iFluor(TM) 750, PE/Texas Red(R), PerCP, PerCP/Cy5.5. Small Molecules: Biotin. Traditional Dyes: FITC (Fluorescein), TRITC (Rhodamine), PacBlue, PacOrange, Cy3, Cy5. iFluor: 350, 405, 430, 450, 488, 514, 532, 546, 555, 560, 568, 594, 610, 633, 647, 660, 670, 680, 700, 710, 750, 790, 800, 810, 820, 840, 860, A7. mFluor: UV375, UV460, Violet 450, Violet 500, Violet 510, Violet 540, Blue 570, Green 620, Red 700, Red 780. Protein 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. Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (PubMed:30146159). [The UniProt Consortium]