| Product Name | VAMP2, 1-94aa, Human |
|---|---|
| Description | VAMP2, also known as vehicle-associated membrane protein 2 isoform 1, which is an integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. VAMP2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25. Recombinant human VAMP2 protein, fused to His-tag at N-terminus, was expressed in E,coli and using conventional chromatography. |
| Synonyms | Vesicle-associated membrane protein 2 isoform 1, VAMP-2, SYB2 |
| Host | Virus |
| Molecular Weight |
52.5kDa (462aa) 50-70kDa (SDS-PAGE under reducing conditions.) |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSHMSATAA TAPPAAPAGE GGPPAPPPNL TSNRRLQQTQ AQVDEVVDIM RVNVDKVLER DQKLSELDDR ADALQAGASQ FETSAAKLKR KYWWKNLK |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol. |
| Concentration | 1.0mg/ml (determined by Absorbance at 280nm) |
| Purity | > 95% 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 | Lin RC., et al. (1997) Neuron. 19(5):1087-94. Hanson PI., et al. (1997) Cell. 90(3):523-35. Scales SJ., et al. (2002) J Biol Chem. 277(31):28271-9. Windoffer R., et al. (1999) Cell Tissue Res. 296(3):499-510. |
| Background | VAMP2, also known as vehicle-associated membrane protein 2 isoform 1, which is an integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. VAMP2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25. Recombinant human VAMP2 protein, fused to His-tag at N-terminus, was expressed in E,coli and using conventional chromatography. |
| Supplier | ARP |
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