This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is the V1 domain F subunit protein. [provided by RefSeq, Jul 2008].
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HEK293T cells were transfected with the pCMV6-ENTRY control (Left lane) or pCMV6-ENTRY ATP6V1F (RC210728, Right lane) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-ATP6V1F.
Western blot analysis of extracts (35ug) from 9 different cell lines by using anti-ATP6V1F monoclonal antibody (HepG2: human; HeLa: human; SVT2: mouse; A549: human; COS7: monkey; Jurkat: human; MDCK: canine; PC12: rat; MCF7: human).
HEK293T cells transfected with either RC210728 overexpress plasmid(Red) or empty vector control plasmid(Blue) were immunostained by anti-ATP6V1F antibody(TA502388), and then analyzed by flow cytometry.
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