VAMP2 Human
Description
Product Specs
Product Science Overview
Synaptobrevin-2 is characterized by its proline-rich N-terminal part, a highly conserved hydrophilic domain, a transmembrane anchor, and a C-terminal . It is one of the key proteins involved in the formation of the SNARE complex, which consists of four α-helices: one contributed by synaptobrevin, one by syntaxin, and two by SNAP-25 (Synaptosome-Associated Protein 25) .
The primary function of Synaptobrevin-2 is to mediate the fusion of synaptic vesicles with the plasma membrane, facilitating the release of neurotransmitters into the synaptic cleft. This process is triggered by an influx of calcium ions (Ca²⁺) into the nerve terminal following an action potential .
During synaptic vesicle fusion, Synaptobrevin-2 forms a complex with the plasma membrane SNARE proteins, syntaxin 1 and SNAP-25. This complex brings the vesicle and plasma membranes into close proximity, allowing them to fuse and release their contents . The tight coupling of the SNARE motif to the transmembrane region of Synaptobrevin-2 is crucial for this process, ensuring efficient Ca²⁺-triggered exocytosis .
Synaptobrevin-2 is targeted by various bacterial toxins, such as tetanospasmin from Clostridium tetani, which causes tetanus, and botulinum toxin from Clostridium botulinum, which causes botulism. These toxins cleave Synaptobrevin-2, disrupting neurotransmitter release and leading to severe neurological symptoms .
Human recombinant Synaptobrevin-2 is produced using recombinant DNA technology, which involves inserting the gene encoding Synaptobrevin-2 into a suitable expression system, such as bacteria or yeast. This allows for the production of large quantities of the protein for research and therapeutic purposes .
