Monoclonal Anti-ATP6V1A, (C-terminal) antibody produced in mouse

This gene encodes 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. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of two V1 domain A subunit isoforms and is found in all tissues. Transcript variants derived from alternative polyadenylation exist. (provided by RefSeq)

ATP6V1A (NP_001681, 508 a.a. ~ 617 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
TLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAQSDNKITWSIIREHMGDILYKLSSMKFKDPLKDGEAKIKSDYAQLLEDMQNAFRSLED

The vacuolar-ATPases significantly control the internal pH by maintaining it neutral. ATP6V1A (ATPase H⁺ transporting V1 subunit A) is known to be associated with the acidification and intracellular trafficking of secretory granules, endosomes, and lysosomes. Mutations in the gene affect the structure and organisation of V-ATPase, glycosylation of proteins, Golgi trafficking. Mutations can also affect the lysosomal function and results in abnormal extracellular matrix homeostasis. ATP6V1A might serve as a prognostic factor in gastric cancer.

Solution in phosphate buffered saline, pH 7.4

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