Anti-VMAT2 / SLC18A2, clone SLC18A2/7983

1 mg/ml in 1X PBS, BSA free, sodium azide free. Neurotransmission depends on the regulated exocytotic release of chemical transmitter molecules. This requires the packaging of these substances into the specialized secretory vesicles of neurons and neuroendocrine cells, a process mediated by specific vesicular transporters. The family of genes encoding the vesicular transporters of monoamines (VMAT 1 and VMAT 2) and acetylcholine (VACht) have been cloned and functionally characterized. The sequence of these integral membrane proteins predicts twelve transmembrane domains and weak homology to a class of bacterial antibiotic resistance proteins. The vesicular transport of neurotransmitter molecules has been shown to be an active ATP- and proton dependent transport mechanism. Protein function: Electrogenic antiporter that exchanges one cationic monoamine with two intravesicular protons across the membrane of secretory and synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to accumulate high concentrations of monoamines inside the vesicles prior to their release via exocytosis. Transports a variety of catecholamines such as dopamine, adrenaline and noradrenaline, histamine, and indolamines such as serotonin (PubMed:8643547, PubMed:23363473). Regulates the transvesicular monoaminergic gradient that determines the quantal size. Mediates somatodendritic dopamine release in hippocampal neurons, likely as part of a regulated secretory pathway that integrates retrograde synaptic signals. Acts as a primary transporter for striatal dopamine loading ensuring impulse-dependent release of dopamine at the synaptic cleft. Responsible for histamine and serotonin storage and subsequent corelease from mast cell granules (PubMed:8860238). [The UniProt Consortium]