Vesicle-Associated Membrane Protein Family

Vesicle-associated membrane proteins (VAMPs), also termed synaptobrevins, are a group of SNARE (soluble N-ethylmaleimide-sensitive factor activating protein receptor) proteins with similar structure. VAMP is anchored to the synaptic vesicle through a single transmembrane domain and has a cytoplasmic domain which contributes a coiled-coil strand to the core complex. VAMPs can form a stable complex with syntaxin, synaptosomal-associated protein and synaptotagmin. They reside on exocytotic vesicles and are mostly involved in the targeting and/or fusion of transport vesicles to their target membrane, by interacting with the plasma membrane proteins SNAP-25 and syntaxin. VAMPs are supposed to be implicated in a late stage of membrane fusion and appose the two membranes to induce an activated docked state and drive vesicle fusion.

Furthermore, VAMP-related membrane fusion appears to be shared with many forms of intracellular trafficking in which homologous proteins perform to fuse a vesicle with its target membrane. Here, we give further details about a part of the vesicle-associated membrane proteins that may be of your interest.

Human Vesicle-associated Membrane Protein Members

Taking advantage of our Magic™ membrane protein production platform, scientists in Creative Biolabs are expert in providing the preparation services of these membrane proteins given above in required formats through different strategies, including detergent micelles, proteoliposomes, nanodiscs, lipoparticles, polymers, with stable cell line.

Magic™ membrane protein production platform – Creative Biolabs

In addition, Magic™ membrane protein antibody discovery platform in Creative Biolabs can be applied in developing antibodies against these targets, even fully humanized antibodies, by various approaches including hybridoma technology, phage display technology, and etc. We also present DNA immunization service for anti-membrane protein antibody development. Please feel free to contact us for more details.

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