Release of neurotransmitters from neurons is regulated by exocytosis of synaptic vesicles. This exocytosis is mediated by a complex consisting of membrane components of both the synaptic vesicle and the synaptic plasma membrane. The fusion complex consists of the soluble NSF (N-ethyl-maleimide-sensitive factor) and SNAPs (soluble NSF attachment proteins), along with the receptor proteins (known as SNAREs) synaptobrevin, synaptotagmin, syntaxin, and SNAP-25 (synaptosomal-associated protein of 25 kDa- the name is coincidental to the previously mentioned "SNAP" terminology). SNAP-25 and syntaxin are plasmalemmal proteins (designated as t-SNAREs) while synaptobrevin and synaptotagmin are vesicular proteins (designated as v-SNAREs). These four proteins are thought to constitute an initial SNARE docking complex for regulated exocytosis. SNAP-25 lacks a transmembrane domain, but is linked to the membrane by palmitoylated cysteine residues in the central region of the molecule.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.