|Other Names||V-type proton ATPase subunit D, V-ATPase subunit D, V-ATPase 28 kDa accessory protein, Vacuolar proton pump subunit D, ATP6V1D, ATP6M, VATD|
|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. 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). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium.|
|Cellular Location||Membrane; Peripheral membrane protein; Cytoplasmic side. Note=Localizes to centrosome and the base of the cilium|
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Provided below are standard protocols that you may find useful for product applications.
ATP6V1D 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.
Smith, A.N., et al. J. Bioenerg. Biomembr. 40(4):371-380(2008)Morel, N. Biol. Cell 95(7):453-457(2003)Smith, A.N., et al. Mol. Cell 12(4):801-803(2003)Kawasaki-Nishi, S., et al. FEBS Lett. 545(1):76-85(2003)
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