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V-ATPase C2 Rabbit Polyclonal Antibody
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V-ATPase C2 Rabbit Polyclonal Antibody

APRab19734-20μL · 20μL

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Catalog No: APRab19734-20μL
Pack Size: 20μL
Brand: EnkiLife

Description

EnkiLife offers the V-ATPase C2 Rabbit Polyclonal Antibody. This antibody reacts with Human,Rat,Mouse species and is suitable for WB,ELISA application. Alternative Names of Immunogen: ATP6V1C2; V-type proton ATPase subunit C 2; V-ATPase subunit C 2; Vacuolar proton pump subunit C 2. The product boasts remarkable high specificity, outstanding reproducibility, and exceptional affinity, making it a reliable and superior choice for your needs. Dilution Ratio: WB 1:500-1:2000,ELISA 1:10000-1:20000 Background: 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,three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. This gene encodes alternate transcriptional splice variants, encoding different V1 domain C subunit isoforms. [provided by RefSeq, Jul 2008],function:Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.,similarity:Belongs to the V-ATPase C subunit family.,subunit:V-ATPase is an heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d).,tissue specificity:Kidney and placenta., Research Area: Oxidative phosphorylation;Vibrio cholerae infection;Epithelial cell signaling in Helicobacter pylori infection;

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