|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||11438 Da|
|Other Names||Vesicle-associated membrane protein 8, VAMP-8, Endobrevin, EDB, VAMP8|
|Target/Specificity||A synthetic peptide corresponding to residues near the N-terminus of human VAMP8 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||VAMP8 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||SNAREs, Soluble N-ethylmaleimide-sensitive factor- attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Also required for dense-granule secretion in platelets. Plays also a role in regulated enzyme secretion in pancreatic acinar cells. Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells. Involved in the homotypic fusion of early and late endosomes.|
|Cellular Location||Lysosome membrane; Single-pass type IV membrane protein. Late endosome membrane; Single-pass type IV membrane protein Note=Perinuclear vesicular structures of the early and late endosomes, coated pits, and trans-Golgi. Sub-tight junctional domain in retinal pigment epithelium cells. Midbody region during cytokinesis. Lumenal oriented, apical membranes of nephric tubular cell. Cycles through the apical but not through the basolateral plasma membrane. Apical region of acinar cells; in zymogen granule membranes (By similarity).|
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Provided below are standard protocols that you may find useful for product applications.
Synaptobrevins/vesicle-associated membrane proteins (VAMPs) together with syntaxins and a synaptosome-associated protein of 25 kDa (SNAP-25) are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane (1). The terminal step of cytokinesis in animal cells is the abscission of the midbody, a cytoplasmic bridge that connects the two prospective daughter cells. It has been shown that two members of the SNARE membrane fusion machinery, syntaxin 2 and endobrevin/VAMP8, specifically localize to the midbody during cytokinesis in mammalian cells (2). It has been established that VAMP8/endobrevin is a major player in regulated exocytosis of the exocrine pancreas. VAMP8 is enriched on the membrane of zymogen granules and exists in a complex with syntaxin 4 and SNAP-23. Results suggest a major physiological role of VAMP8 in regulated exocytosis of pancreatic acinar cells by serving as a v-SNARE of zymogen granules (3).
1. Wong SH et al. Mol Biol Cell 9(6):1549-63, 1998
2. Low SH et al. Dev Cell 4(5):753-9, 2003
3. Wang CC, et al. Dev Cell 7(3):359-71, 2004
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