Description
ATP6V1A Antibody | 15-677 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human, Mouse, Rat
Homology: N/A
Immunogen: A synthetic peptide corresponding to a sequence within amino acids 500-600 of human ATP6V1A (NP_001681.2) .
Research Area: Signal Transduction
Tested Application: WB, IHC
Application: WB: 1:500 - 1:2000
IHC: 1:100 - 1:200
Specificiy: N/A
Positive Control 1: 293T
Positive Control 2: LO2
Positive Control 3: HeLa
Positive Control 4: Mouse brain
Positive Control 5: Mouse heart
Positive Control 6: Mouse kidney
Molecular Weight: Observed: 68kDa
Validation: N/A
Isoform: N/A
Purification: Affinity purification
Clonality: Polyclonal
Clone: N/A
Isotype: IgG
Conjugate: Unconjugated
Physical State: Liquid
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Concentration: N/A
Storage Condition: Store at -20˚C. Avoid freeze / thaw cycles.
Alternate Name: V-type proton ATPase catalytic subunit A, V-ATPase subunit A, V-ATPase 69 kDa subunit, Vacuolar ATPase isoform VA68, Vacuolar proton pump subunit alpha, ATP6V1A, ATP6A1, ATP6V1A1, VPP2
User Note: Optimal dilutions for each application to be determined by the researcher.
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 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.