The Synaptic Vesicle Antibody Sampler Kit provides an economical means of evaluating proteins involved in synaptic vesicle fusion and membrane trafficking. The kit contains enough primary and secondary antibodies to perform four western miniblot experiments with each antibody.
Munc18-1 (D4O6V) Rabbit mAb recognizes endogenous levels of total Munc18-1 protein. NSF (D31C7) XP® Rabbit mAb detects endogenous levels of total NSF protein. SNAP25 (D9A12) Rabbit mAb detects endogenous levels of total SNAP25 protein. Syntaxin 6 (C34B2) Rabbit mAb detects endogenous levels of total syntaxin 6 protein.
Monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Tyr157 of human Munc18-1 protein, residues surrounding Tyr140 of mouse syntaxin 6 protein, residues surrounding Gln116 of human SNAP25 protein, or residues surrounding Leu524 of human NSF protein.
Fusion of a vesicle to its target membrane is a universal process in eukaryotic cells for proper cellular organization and function. Several protein-protein interactions are essential to membrane fusion during endocytosis. Membrane fusion requires interaction among SNARE1 proteins associated with both donor and acceptor membranes (1,2). SNAP25 forms a core complex with the SNARE proteins syntaxin and synaptobrevin to mediate synaptic vesicle fusion with the plasma membrane during Ca2+-dependent exocytosis (3). Syntaxin 6 is a ubiquitously expressed S25C family member of the SNARE proteins (4,5). Munc18-1 acts as a molecular chaperone for syntaxin-1, allowing for formation of the SNARE complex at the plasma membrane (6). Following membrane fusion, the α-SNAP cytoplasmic adapter protein binds to the SNARE complex. N-ethylmaleimide-sensitive factor (NSF), a hexameric ATPase, then associates with the α-SNAP/SNARE complex to mediate SNARE disassembly during membrane fusion (7,8). The ATPase activity of NSF induces a conformational change in the α-SNAP/SNARE complex that leads to its dissociation from the membrane, membrane fusion, and eventual recycling of the SNARE complex for subsequent membrane fusion (7,8).
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