|Other Names||V-type proton ATPase 16 kDa proteolipid subunit, V-ATPase 16 kDa proteolipid subunit, Vacuolar proton pump 16 kDa proteolipid subunit, ATP6V0C, ATP6C, ATP6L, ATPL|
|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.|
|Synonyms||ATP6C, ATP6L, ATPL|
|Function||Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.|
|Cellular Location||Vacuole membrane; Multi-pass membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
ATP6V0C is a component of vacuolar ATPase(V-ATPase), a multisubunit enzyme that mediates acidification ofeukaryotic intracellular organelles. V-ATPase dependent organelleacidification is necessary for such intracellular processes asprotein sorting, zymogen activation, receptor-mediated endocytosis,and synaptic vesicle proton gradient generation. V-ATPase iscomposed of a cytosolic V1 domain and a transmembrane V0 domain.The V1 domain consists of three A and three B subunits, two Gsubunits plus the C, D, E, F, and H subunits. The V1 domaincontains the ATP catalytic site. The V0 domain consists of fivedifferent subunits: a, c, c', c', and d. ATP6V0C encodes the V0subunit c.
O'Callaghan, K.M., et al. J. Biol. Chem. 285(1):381-391(2010)You, H., et al. Cancer Lett. 280(1):110-119(2009)Lee, I., et al. J. Biol. Chem. 279(51):53007-53014(2004)Morel, N. Biol. Cell 95(7):453-457(2003)Smith, A.N., et al. Mol. Cell 12(4):801-803(2003)
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