SNAP23 is structurally and functionally similar to SNAP25, another member of the SNARE family. It binds tightly to multiple syntaxins and synaptobrevins/VAMPs, forming a complex that serves as a binding site for the general membrane fusion machinery . This protein is essential for the high-affinity receptor involved in the docking and fusion of transport vesicles .
Unlike SNAP25, which is predominantly found in the brain, SNAP23 is ubiquitously expressed in various tissues, including the plasma membrane and other intracellular membranes . This widespread expression allows SNAP23 to facilitate exocytotic membrane fusion in most cells that do not express SNAP25 .
SNAP23 is involved in several critical cellular processes, including:
Recombinant human SNAP23 protein is produced using various expression systems, such as Escherichia coli, to achieve high purity and functionality . This recombinant protein is used in research to study the mechanisms of vesicular transport and membrane fusion, as well as in the development of diagnostic and therapeutic applications .