VAMP2 Antibody

Synaptobrevin-2, also known as Vesicle-associated membrane protein 2 (VAMP2), is a crucial component of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex. This protein plays a pivotal role in the process of membrane fusion, which is essential for neurotransmitter release at synapses .

Synaptobrevin-2 is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicles . It consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal . The protein is largely unstructured in the absence of interaction partners but stabilizes upon interaction with other SNARE proteins, forming a four-helix bundle .

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 critical for the transmission of signals between neurons in the central nervous system (CNS) .

In addition to its role in neurotransmitter release, Synaptobrevin-2 is also implicated in the secretion of antibodies by human plasma cells . It interacts with other SNARE proteins such as SNAP23 and STX4 to mediate the fusion of vesicles carrying antibodies with the plasma membrane .

Synaptobrevin-2 is targeted by various bacterial toxins, including tetanospasmin from Clostridium tetani and botulinum toxin from Clostridium botulinum . These toxins cleave Synaptobrevin-2, disrupting neurotransmitter release and leading to conditions such as tetanus and botulism .

The Mouse Anti Human Synaptobrevin-2 antibody is a monoclonal antibody derived from the hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human VAMP2 . This antibody is used in various laboratory research applications, including ELISA and Western blot analysis, to study the expression and function of Synaptobrevin-2 .