Technical Data
032295
ATP6V0C, CT (ATP6V0C, ATP6C, ATP6L, ATPL, V-type proton ATPase 16kD proteolipid subunit, Vacuolar proton pump 16kD proteolipid subunit)
Description:
ATP6V0C is 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. ATP6V0C encodes the V0 subunit c.

Applications:
Suitable for use in Western Blot, ELISA

Recommended Dilution:
ELISA: 1:1,000
Western Blot: 1:100-500

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
PabIgGAffinity Purified
SizeStorageShippingSourceHost
200ul-20CBlue IceHumanRabbit
Concentration:
As reported
Immunogen:
ATP6V0C antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 107-134 amino acids from the C-terminal region of human ATP6V0C.
Purity:
Purified by Protein A affinity chromatography.
Form
Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide.
Specificity:
Human, mouse
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
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)