ATP6V0A4 Blocking Peptide (Center)
€293.00
In stock
SKU
AC-BP5369c
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.
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
Type: Synthetic peptide
Primary Accession: Q9HBG4
Other Accession: NP_570856.2;NP_570855.2
Gene ID: 50617
Gene Name: ATP6V0A4
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.
Bio 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) :
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.
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
Type: Synthetic peptide
Primary Accession: Q9HBG4
Other Accession: NP_570856.2;NP_570855.2
Gene ID: 50617
Gene Name: ATP6V0A4
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.
Bio 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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