VAMP3, also known as cellubrevin or synaptobrevin-3, is a ubiquitously expressed vesicular-SNARE protein critical for intracellular membrane fusion events. It facilitates the trafficking of recycling endosomes, secretory granules, and cytokines in immune cells like mast cells (MCs) and macrophages . VAMP3 interacts with syntaxins (e.g., STX4, STX6) and SNAP23 to mediate granule-plasma membrane fusion, influencing processes such as MC degranulation and phagocytosis .
VAMP3 antibodies have been instrumental in elucidating the protein’s role in cellular processes:
Mechanism: VAMP3 mediates granule-to-granule fusion in IgE/Ag-activated MCs, enabling rapid β-hexosaminidase release. Knockdown (KD) reduces early-phase degranulation but enhances FcεRI signaling (e.g., Ca²⁺ influx, ERK phosphorylation) .
Cytokine Regulation: VAMP3 KD increases IL-6 secretion but reduces TNF-α release in MCs, highlighting its role in balancing inflammatory outputs .
Kidney Function: VAMP3 interacts with NKCC2 in renal thick ascending limbs (TALs). VAMP3⁻/⁻ mice exhibit reduced NKCC2 surface expression, impairing urine concentration .
Pathogen Interactions: VAMP3 localizes to Chlamydia trachomatis inclusions in host cells, facilitating inclusion expansion via chlamydial protein synthesis .
Vamp3 regulates endocytic brain-derived neurotrophic factor (BDNF) release in astrocytes, impacting neuronal plasticity .
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.