ATP6V0A2 antibody [N1N3]
![Research Use Only](static/images/certificates/ruo.jpg)
GTX111275
Overview
- SupplierGeneTex
- Product NameATP6V0A2 antibody [N1N3]
- Delivery Days Customer9
- Application Supplier NoteWB: 1:500-1:3000. *Optimal dilutions/concentrations should be determined by the researcher.Not tested in other applications.
- ApplicationsWestern Blot
- CertificationResearch Use Only
- ClonalityPolyclonal
- Concentration0.89 mg/ml
- ConjugateUnconjugated
- FormulationLiquid
- Gene ID23545
- Target nameATP6V0A2
- Target descriptionATPase H+ transporting V0 subunit a2
- Target synonymsA2; a2V; A2V-ATPase; ARCL; ARCL2A; ATP6A2; ATP6N1D; ATPase, H+ transporting, lysosomal V0 subunit a2; J6B7; lysosomal H(+)-transporting ATPase V0 subunit a2; regeneration and tolerance factor; RTF; STV1; TJ6; TJ6M; TJ6S; vacuolar proton translocating ATPase 116 kDa subunit a; V-ATPase 116 kDa subunit a2; V-ATPase subunit a2; VPH1; v-type proton ATPase 116 kDa subunit a; V-type proton ATPase 116 kDa subunit a2; WSS
- HostRabbit
- IsotypeIgG
- Protein IDQ9Y487
- Protein NameV-type proton ATPase 116 kDa subunit a isoform 2
- Scientific DescriptionThe multisubunit vacuolar-type proton pump (H(+)-ATPase or V-ATPase) is essential for acidification of diverse cellular components, including endosomes, lysosomes, clathrin-coated vesicles, secretory vesicles, and chromaffin granules, and it is found at high density in the plasma membrane of certain specialized cells. H(+)-ATPases are comprised of a peripheral V(1) domain and an integral membrane V(0) domain; ATP6V0A2 is a component of the V(0) domain (Smith et al., 2003 [PubMed 14580332]).[supplied by OMIM]
- ReactivityHuman
- Storage Instruction-20°C or -80°C,2°C to 8°C
- UNSPSC12352203
References
- Comparative Nucleotide-Dependent Interactome Analysis Reveals Shared and Differential Properties of KRas4a and KRas4b. Zhang X et al., 2018 Jan 24, ACS Cent SciRead more
- mTORC1 and muscle regeneration are regulated by the LINC00961-encoded SPAR polypeptide. Matsumoto A et al., 2017 Jan 12, NatureRead more