| Product Name | ATP6V1F, 1-119aa, Human |
|---|---|
| Description | ATP6V1F 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. 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. Recombinant human ATP6V1F, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | V-type proton ATPase subunit F, V-type proton ATPase subunit F, ATP6S14, VATF, Vma7 |
| Host | E. coli |
| Molecular Weight | 32.0 kDa (383aa) |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSMAGRGKL IAVIGDEDTV TGFLLGGIGE LNKNRHPNFL VVEKDTTINE IEDTFRQFLN RDDIGIILIN QYIAEMVRHA LDAHQQSIPA VLEIPSKEHP YDAAKDSILR RARGMFTAED LR |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl (pH8.0) containing 10% glycerol |
| Concentration | 0.25 mg/ml (determined by Bradford assay) |
| Purity | > 90% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Supino R., et al. (2009) Ann. N. Y. Acad. Sci. 1171, 606-616 Smith AN., et al. (2008) J. Bioenerg. Biomembr. 40 (4), 371-380 |
| Background | ATP6V1F 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. 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. Recombinant human ATP6V1F, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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