| Product Name | VAMP8, 1-76aa, Human, Recombinant |
|---|---|
| Description | Vehicle-associated membrane (VAMP8) ,also known as endobrevin, is the main components of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. This protein plays a role in regulated enzyme secretion in pancreatic acinar cells and is involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells. It is required for dense-granule secretion in platelets. Recombinant VAMP8 protein was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | Endobrevin, EDB, VAMP8, Vesicle-associated membrane protein 8, Vesicle-associated membrane protein 8 VAMP 5, VAMP 8, VAMP-8, VAMP5, Vesicle associated membrane protein 8. |
| Host | E. coli |
| Molecular Weight | 17.9 kDa (154 aa), confirmed by MALDI-TOF. |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MEEASEGGGN DRVRNLQSEV EGVKNIMTQN VERILARGEN LEHLRNKTED LEATSEHFKT TSQKVARKFW WKNVKM |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 50 mM HEPES (pH7.5) 150 mM NaCl, 1mM DTT, 10% glycerol |
| Concentration | 1 mg/ml (determined by Bradford assay) |
| Purity | > 85% by SDS PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Polgar J., et al. (2002) Blood. 100(3):1081-3. Ren Q., et al. (2007) Mol Biol Cell. 18(1):24-33 |
| Background | Vehicle-associated membrane (VAMP8) ,also known as endobrevin, is the main components of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. This protein plays a role in regulated enzyme secretion in pancreatic acinar cells and is involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells. It is required for dense-granule secretion in platelets. Recombinant VAMP8 protein was expressed in E.coli and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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