|Other Accession||NP_570856.2, NP_570855.2|
|Other Names||V-type proton ATPase 116 kDa subunit a isoform 4, V-ATPase 116 kDa isoform a4, Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4, Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform, ATP6V0A4, ATP6N1B, ATP6N2|
|Target/Specificity||The synthetic peptide sequence is selected from aa 250-261 of HUMAN ATP6V0A4|
|Format||Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.|
|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||Part of the proton channel of the V-ATPase that is involved in normal vectorial acid transport into the urine by the kidney.|
|Cellular Location||Apical cell membrane; Multi-pass membrane protein. Note=Present at high density almost exclusively on the apical surface of alpha-intercalated cells in the cortical collecting ducts of the distal nephron|
|Tissue Location||Expressed in adult and fetal kidney. Found in the inner ear.|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular compartments of eukaryotic cells. V-ATPase dependent 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. This gene is one of four genes in man and mouse that encode different isoforms of the a subunit. Alternatively spliced transcript variants encoding the same protein have been described. Mutations in this gene are associated with renal tubular acidosis associated with preserved hearing.
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Su, Y., et al. Am. J. Physiol. Renal Physiol. 295 (4), F950-F958 (2008) :
Norgett, E.E., et al. J. Biol. Chem. 282(19):14421-14427(2007)
Smith, A.N., et al. J. Am. Soc. Nephrol. 16(5):1245-1256(2005)
Forgac, M. J. Biol. Chem. 274(19):12951-12954(1999)
Nelson, N., et al. Physiol. Rev. 79(2):361-385(1999)
Kane, P.M. J. Bioenerg. Biomembr. 31(1):3-5(1999)
Finbow, M.E., et al. Biochem. J. 324 (PT 3), 697-712 (1997) :
Stevens, T.H., et al. Annu. Rev. Cell Dev. Biol. 13, 779-808 (1997) :
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