VAMP2 (Synaptobrevin 2) is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, and consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. Synaptobrevin 2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein (residues 1-89) forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25.
VAMP2 is produced in E.Coli as a single, non-glycosylated polypeptide chain containing 126 amino acids (1-89) and having a molecular mass of 13.8 kDa. VAMP contains 37 amino acids His-Tag fused at N-terminus and purified by standard chromatography techniques. Purity is >95.0% as determined by SDS-PAGE.
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