Anti-ATP6V1E2 monoclonal antibody Made to order

Antibody Isotype

IgG

Species Reactivity

Human

Immunogen

A synthetic peptide of human ATP6V1E2 is used for rabbit immunization.

Conjugate

Alternative Names

ATP6V1E2; ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E2; VMA4; ATP6E1; ATP6EL2; ATP6V1EL2; V-type proton ATPase subunit E 2; V-ATPase subunit E 2; vacuolar proton pump subunit E 2; vacuolar-type proton-translocating ATPase subunit E1;

Entrez Gene ID

UniProt ID

Antigen Description

H+-ATPase (also known as vacuolar ATPase, V-ATPase) is a enzyme transporter that functions to acidify
intracellular compartments in eukaryotic cells. It is ubiquitously expressed and is present in endomembrane
organelles such as vacuoles, lysosomes, endosomes, the Golgi apparatus, chromaffin granules and coated
vesicles, as well as in the plasma membrane. H+-ATPase is a multisubunit complex composed of two domains.
The V1 domain is responsible for ATP hydrolysis and the V0 domain is responsible for protein translocation.
There are two main mechanisms of regulating H+-ATPase activity; recycling of H+-ATPase-containing vesicles
to and from the plasma membrane and glucose-sensitive assembly/disassembly of the holoenzyme complex. These
transporters play an important role in processes such as receptor-mediated endocytosis, protein degradation
and coupled transport. They have a function in bone reabsorption and mutations in the A3 gene cause
recessive osteopetrosis. Furthermore, H+-ATPases have been implicated in tumor metastasis and regulation of
sperm motility and maturation.

Pathway

Collecting duct acid secretion; Collecting duct acid secretion; Disease; Epithelial cell signaling in Helicobacter pylori infection; Epithelial cell signaling in Helicobacter pylori infection; Insulin receptor recycling; Iron uptake and transport; Latent infection of Homo sapiens with Mycobacterium tuberculosis; Oxidative phosphorylation; Oxidative phosphorylation; Phagosomal maturation (early endosomal stage);