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ATP6V0A4 Antibody (Center)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| FC, WB, E |
|---|---|
| Primary Accession | Q9HBG4 |
| Other Accession | NP_570856.2, NP_570855.2 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 96386 Da |
| Antigen Region | 235-261 aa |
| Gene ID | 50617 |
|---|---|
| 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 | This ATP6V0A4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 235-261 amino acids from the Central region of human ATP6V0A4. |
| Dilution | WB~~1:1000 FC~~1:10~50 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | ATP6V0A4 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ATP6V0A4 |
|---|---|
| Synonyms | ATP6N1B, ATP6N2 |
| Function | Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Involved in normal vectorial acid transport into the urine by the kidney (PubMed:10973252, PubMed:12414817). |
| Cellular Location | Apical cell membrane; Multi-pass membrane protein. Basolateral cell membrane {ECO:0000250|UniProtKB:Q920R6}; Multi-pass membrane protein. Note=Localizes to the apical surface of alpha- intercalated cells in the cortical collecting ducts of the distal nephron (PubMed:10973252). Localizes to the basolateral surface of beta-intercalated cells in the cortical collecting ducts of the distal nephron (By similarity). {ECO:0000250|UniProtKB:Q920R6, ECO:0000269|PubMed:10973252} |
| 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.
Background
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.
References
Andreucci, E., et al. Pediatr. Nephrol. 24(11):2147-2153(2009)
Hinton, A., et al. J. Biol. Chem. 284(24):16400-16408(2009)
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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