ATP6V1C2 Mouse Monoclonal Antibody [Clone ID: OTI2H3]

Specifications

Product Data
Clone Name	OTI2H3
Applications	IHC, WB
Recommend Dilution	WB 1:2000, IHC 1:150
Reactivity	Human, Mouse, Rat
Host	Mouse
Clonality	Monoclonal
Immunogen	Full length human recombinant protein of human ATP6V1C2(NP_653184) produced in E.coli.
Formulation	Lyophilized powder (original buffer 1X PBS, pH 7.3, 8% trehalose)
Reconstitution Method	For reconstitution, we recommend adding 100uL distilled water to a final antibody concentration of about 1 mg/mL. To use this carrier-free antibody for conjugation experiment, we strongly recommend performing another round of desalting process. (OriGene recommends Zeba Spin Desalting Columns, 7KMWCO from Thermo Scientific)
Purification	Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)
Conjugation	Unconjugated
Storage Condition	Store at -20°C as received.
Predicted Protein Size	43.7 kDa
Gene Name	ATPase H+ transporting V1 subunit C2
Database Link	NP_653184 Entrez Gene 68775 MouseEntrez Gene 362802 RatEntrez Gene 245973 Human UniProt ID Q8NEY4
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]
Synonyms	ATP6C2; VMA5
Reference Data
Protein Pathways	Epithelial cell signaling in Helicobacter pylori infection, Metabolic pathways, Oxidative phosphorylation, Vibrio cholerae infection

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