Recombinant VAMP7 protein (His tag)

• DataSheet
• Material Safety Data Sheets (MSDS)

Introducing our high-quality recombinant human VAMP7 protein fragment (amino acids 2-188), designed for researchers studying vesicle trafficking and membrane fusion mechanisms. This fragment fully encompasses the critical Longin and v-SNARE coiled-coil homology domains, making it an ideal tool for investigating specific domain functions in intracellular transport processes.

Vesicle-associated membrane protein 7 (VAMP-7) is a key regulator of intracellular membrane trafficking in human cells. This tetanus-insensitive VAMP plays crucial roles in targeting and fusion of transport vesicles during protein transport from early endosomes to lysosomes. VAMP-7 is essential for both heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion, and it mediates calcium-regulated lysosomal exocytosis. The protein also facilitates chylomicron export from the endoplasmic reticulum to the cis Golgi, supports exocytosis during immune cell degranulation (eosinophils, neutrophils, and natural killer cells), and enables focal exocytosis during phagosome formation. VAMP-7 localizes to multiple intracellular membranes including secretory vesicles, trans-Golgi network, late endosomes, lysosomes, endoplasmic reticulum, and phagosomes, functioning as a single-pass type IV membrane protein that orchestrates critical membrane fusion events throughout the endolysosomal pathway.