VAMP-2 / Synaptobrevin-2 antibody

Background of VAMP-2 / Synaptobrevin-2 antibody

VAMP-2 (also known as syptobrevin-2) is a member of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SRE) protein superfamily. The family includes 36 members in humans and is characterized by the SRE motif, an evolutiorily conserved stretch of 60â??70 amino acids that are arranged in heptad repeats. SRE proteins are involved in exocytosis and intracellular vesicle trafficking and are essential for cell growth, hormone secretion and neurotransmission, processes that require rapid, targeted, and regulated membrane fusion. SREs can be roughly divided into vesicular (v-SREs) and target (t-SREs) based on their distribution on the transport vesicle or target membrane respectively. Thus, assembly of cogte v-/t-SREs between two opposing membranes generates trans-SRE complexes, which bring the lipid bilayers in close proximity and drive membrane fusion. VAMP-2, like most SREs, is a type IV membrane protein with a relatively large N-terminus containing the SRE motif located in the cytoplasmic side and a transmembrane domain located close to the C-terminus that functions as an anchor. VAMP-2 has been extensively studied for its role on neurol and neuroendocrine cell exocytosis where it functions as the vesicle membrane protein v-SRE, which together with the plama membrane t-SRE protein Syntaxin 1 and the membrane-associated SP-25 (syptosome-associated protein 25 kDa), forms a trimeric, four-helical complex, which drives fusion of the two opposing bilayers. VAMP-2 is the target of the tetanus neurotoxin (TeNT) and of several botulinum neurotoxin (BoNT) types: type B, D, F, and G. The neurotoxins cause specific proteolytic degradation of the VAMP-2 protein, which in turn causes SRE complex disruption and inhibition of neurotransmitter release.