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V-ATPase C2 Polyclonal Antibody, 50ul Cell fragmentation and collection This enzyme also demonstrates glutathione-dependent

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V-ATPase C2 Polyclonal Antibody, 50ul Cell fragmentation and collection This enzyme also demonstrates glutathione-dependentATP6V1C2 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

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Description

This enzyme also demonstrates glutathione-dependent peroxidase activity towards lipid hydroperoxides

Knockout studies in mice suggest that PTGES may contribute to the pathogenesis of collagen-induced arthritis and mediate acute pain during inflammatory responses

a transmembrane region and a truncated cytoplasmic domain but lacks the prosequence and tripeptide HAV adhesion recognition sequence typical of most classical cadherins

a consensus furin cleavage site

additionally suggesting a metabolic function for the protein

V-ATPase C2 Polyclonal Antibody, 50ul Cell fragmentation and collection This enzyme also demonstrates glutathione-dependentATP6V1C2 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

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