ATP6V1A antibody
![Research Use Only](static/images/certificates/ruo.jpg)
GTX110815
ApplicationsImmunoPrecipitation, Western Blot, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
Product group Antibodies
ReactivityHuman, Mouse
TargetATP6V1A
Overview
- SupplierGeneTex
- Product NameATP6V1A antibody
- Delivery Days Customer9
- Application Supplier NoteWB: 1:1000-1:10000. IHC-P: 1:100-1:1000. IP: 1:100-1:500. *Optimal dilutions/concentrations should be determined by the researcher.Not tested in other applications.
- ApplicationsImmunoPrecipitation, Western Blot, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
- CertificationResearch Use Only
- ClonalityPolyclonal
- Concentration0.57 mg/ml
- ConjugateUnconjugated
- FormulationLiquid
- Gene ID523
- Target nameATP6V1A
- Target descriptionATPase H+ transporting V1 subunit A
- Target synonymsARCL2D; ATP6A1; ATP6V1A1; ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A; ATPase, H+ transporting, lysosomal, subunit A1; DEE93; H(+)-transporting two-sector ATPase, subunit A; H+-transporting ATPase chain A, vacuolar (VA68 type); HO68; IECEE3; VA68; vacuolar proton pump alpha subunit 1; vacuolar proton pump subunit alpha; V-ATPase 69 kDa subunit 1; V-ATPase A subunit 1; V-ATPase subunit A; Vma1; VPP2; V-type proton ATPase (V-ATPase) catalytic subunit A; V-type proton ATPase catalytic subunit A
- HostRabbit
- IsotypeIgG
- Protein IDP38606
- Protein NameV-type proton ATPase catalytic subunit A
- Scientific DescriptionThis 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 one of two V1 domain A subunit isoforms and is found in all tissues. Transcript variants derived from alternative polyadenylation exist. [provided by RefSeq]
- ReactivityHuman, Mouse
- Storage Instruction-20°C or -80°C,2°C to 8°C
- UNSPSC12352203
References
- Faulty autolysosome acidification in Alzheimers disease mouse models induces autophagic build-up of Abeta in neurons, yielding senile plaques. Lee JH et al., 2022 Jun, Nat NeurosciRead more
- Fronto-temporal dementia risk gene TMEM106B has opposing effects in different lysosomal storage disorders. Perez-Canamas A et al., 2021, Brain CommunRead more
- Thioredoxin-Interacting Protein Promotes Phagosomal Acidification Upon Exposure to Escherichia coli Through Inflammasome-Mediated Caspase-1 Activation in Macrophages. Yoon SJ et al., 2019, Front ImmunolRead more
- Novel c.G630A TCIRG1 mutation causes aberrant splicing resulting in an unusually mild form of autosomal recessive osteopetrosis. Zirngibl RA et al., 2019 Oct, J Cell BiochemRead more
- TMEM55B contributes to lysosomal homeostasis and amino acid-induced mTORC1 activation. Hashimoto Y et al., 2018 Jun, Genes CellsRead more
- The TMEM127 human tumor suppressor is a component of the mTORC1 lysosomal nutrient-sensing complex. Deng Y et al., 2018 May 15, Hum Mol GenetRead more
- Activity-independent targeting of mTOR to lysosomes in primary osteoclasts. Wang A et al., 2017 Jun 7, Sci RepRead more
- mTORC1 and muscle regeneration are regulated by the LINC00961-encoded SPAR polypeptide. Matsumoto A et al., 2017 Jan 12, NatureRead more
- Neuronal ceroid lipofuscinosis with DNAJC5/CSPalpha mutation has PPT1 pathology and exhibit aberrant protein palmitoylation. Henderson MX et al., 2016 Apr, Acta NeuropatholRead more
- Metabolism. Differential regulation of mTORC1 by leucine and glutamine. Jewell JL et al., 2015 Jan 9, ScienceRead more