Synaptobrevin-3, also known as VAMP3 (Vesicle-Associated Membrane Protein 3), is a member of the SNARE (Soluble NSF Attachment Protein Receptor) protein family. These proteins are essential for the fusion of vesicles with target membranes, a critical process in cellular transport and communication. Synaptobrevin-3 is particularly involved in the exocytosis of synaptic vesicles, playing a vital role in neurotransmitter release at synapses.
Synaptobrevin-3 is a small, integral membrane protein characterized by a single transmembrane domain, a cytoplasmic domain, and a short luminal domain. The cytoplasmic domain contains the SNARE motif, which is crucial for its interaction with other SNARE proteins, such as syntaxin and SNAP-25, to form the SNARE complex. This complex mediates the docking and fusion of synaptic vesicles with the presynaptic membrane, facilitating the release of neurotransmitters into the synaptic cleft .
The primary function of Synaptobrevin-3 is to mediate the fusion of synaptic vesicles with the presynaptic membrane. This process is essential for the release of neurotransmitters, which are chemical messengers that transmit signals between neurons. The SNARE complex, formed by Synaptobrevin-3, syntaxin, and SNAP-25, undergoes a series of conformational changes that bring the vesicle and target membranes into close proximity, ultimately leading to membrane fusion and neurotransmitter release .
The Mouse Anti Human Synaptobrevin-3 antibody is a monoclonal antibody specifically designed to target and bind to the human Synaptobrevin-3 protein. Monoclonal antibodies are produced by identical immune cells that are clones of a unique parent cell, ensuring specificity and consistency in their binding properties. This antibody is widely used in research to study the expression, localization, and function of Synaptobrevin-3 in various biological systems.