Eukaryotic protein trafficking involves the packaging of target molecules into membranous vesicles that bud from a donor compartment, travel to a specific destination, fuse, and release their components into an acceptor compartment. Components of both the vesicle and the synaptic plasma membrane interact to form a fusion complex which mediates specific docking and fusion of vesicles. This complex contains NSF (N-ethyl-maleimide-sensitive factor), SNAPs (soluble NSF attachment proteins), and receptor proteins (SNAREs) that include synaptobrevin, synaptotagmin, syntaxin, and SNAP-25 (synaptosome-associated protein of 25 kDa). SNAP-25 and syntaxin are associated with the target plasma membrane (t-SNAREs), while synaptobrevin and synaptotagmin are vesicle-associated proteins (v-SNAREs). In Drosophila, protein transport from the ER to Golgi involves Bet1p, a v-SNARE. With 28% amino acid identity to Bet1p, GS15 (Golgi SNARE of 15 kDa) is widely expressed in rat tissues. It is an integral membrane protein of the Golgi apparatus and functions as a SNARE. Thus, GS15 is thought to be a novel SNARE that participates in ER-Golgi protein transport through an undefined process.
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.