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Synaptosomal-associated proteins (SNAPs) are cytosolic proteins that play a key role in in the process of membrane fusion in intracellular vesicle trafficking. In eukaryotic cells, the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complex is critical to membrane docking and fusion and is believed to impart some degree of specificity between vesicle SNARE (v-SNARE) and target organelle SNARE (t-SNARE). In neurons and neuroendocrine cells, the SNARE complex consists of the integral membrane proteins VAMP (vesicle-associated membrane protein), syntaxin and SNAP-25. In non-neuronal tissue, a SNAP-25 homolog, SNAP-23, functionally replaces SNAP-25 in the SNARE complex. Studies show that VAMP, syntaxin and SNAP-23 are required for SNARE function and that this complex exists as a heterotrimer of the three proteins. In insulin signalling pathways, studies suggest that the translocation of GLUT4 in adipocytes requires that functional SNAP-23 be present in SNARE complexes.
![Western Blot SNAP23 Antibody [Unconjugated]](http://images.novusbio.com/fullsize/antibody/SNAP23_AF6306_Western_Blot_9825.jpg)
![Immunocytochemistry SNAP23 Antibody [Unconjugated]](http://images.novusbio.com/fullsize/antibody/SNAP23_AF6306_Immunocytochemistry__Immunofluorescence_19176.jpg)
