Anti-ATP6V0A1 antibody produced in rabbit

ATP6V0A1 is 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. ATP6V0A1 is one of three A subunit proteins and it is associated with clathrin-coated vesicles. 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. The occurrence of splice variants encoding different protein products has been reported, but the full-length natures of these transcripts have not been determined. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

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Synthetic peptide directed towards the N terminal region of human ATP6V0A1

Synthetic peptide located within the following region: RDLNPDVNVFQRKFVNEVRRCEEMDRKLRFVEKEIRKANIPIMDTGENPE

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.