ATP6V0E1 (NM_003945) Human Recombinant Protein
Recombinant protein of human ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e1 (ATP6V0E1)
Product Datasheet for 'TP315618'
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|Description||Recombinant protein of human ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e1 (ATP6V0E1)|
|Expression cDNA Clone or AA Sequence||Recombinant protein was produced with TrueORF clone, RC215618. Click on the TrueORF clone link to view cDNA and protein sequences.|
|Predicted MW||9.2 kDa|
|Concentration||>50 ug/mL as determined by microplate BCA method|
|Purity||> 80% as determined by SDS-PAGE and Coomassie blue staining|
|Buffer||25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol. Store at –80C. Avoid repeated freeze-thaw cycles. Stable for 3 months from receipt of products under proper storage and handling conditions.|
|Synonyms||ATP6H; ATP6V0E; M9.2; Vma21; Vma21p|
|Summary||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 possibly part of the V0 subunit. Since two nontranscribed pseudogenes have been found in dog, it is possible that the localization to chromosome 2 for this gene by radiation hybrid mapping is representing a pseudogene. Genomic mapping puts the chromosomal location on 5q35.3. [provided by RefSeq, Jul 2008].|
|Protein Pathways||Oxidative phosphorylation, Metabolic pathways, Vibrio cholerae infection, Epithelial cell signaling in Helicobacter pylori infection|