|Other Names||V-type proton ATPase subunit H, V-ATPase subunit H, Nef-binding protein 1, NBP1, Protein VMA13 homolog, V-ATPase 50/57 kDa subunits, Vacuolar proton pump subunit H, Vacuolar proton pump subunit SFD, ATP6V1H|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity). Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes.|
|Tissue Location||Widely expressed.|
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Provided below are standard protocols that you may find useful for product applications.
ATP6V1H 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 gene encodes the regulatory H subunit of the V1 domain which is required for catalysis of ATP but not the assembly of V-ATPase.
Fuster, D.G., et al. Kidney Int. 73(10):1151-1158(2008)Stove, V., et al. J. Virol. 79(17):11422-11433(2005)Morel, N. Biol. Cell 95(7):453-457(2003)
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