VAMP2 Human, (1-94)
E.Coli
Vesicle Associated Membrane Protein 2, Vesicle-Associated Membrane Protein 2, Synaptobrevin 2, VAMP-2, SYB2, Synaptobrevin-2.
Greater than 95.0% as determined by SDS-PAGE.
Description
VAMP2 Human Recombinant produced in e.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-94 a.a) and having a molecular mass of 12.8kDa. VAMP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Vesicle Associated Membrane Protein 2, Vesicle-Associated Membrane Protein 2, Synaptobrevin 2, VAMP-2, SYB2, Synaptobrevin-2.
E.Coli
MGSSHHHHHH SSGLVPRGSH MGSHMSATAA TAPPAAPAGE GGPPAPPPNL TSNRRLQQTQ AQVDEVVDIM RVNVDKVLER DQKLSELDDR ADALQAGASQ FETSAAKLKR KYWWKNLK.
Product Science Overview
Synaptobrevin-2, also known as Vesicle-Associated Membrane Protein 2 (VAMP2), is a small integral membrane protein that plays a crucial role in the process of synaptic vesicle exocytosis. This protein is part of the SNARE (Soluble NSF Attachment Protein Receptor) complex, which is essential for the fusion of synaptic vesicles with the presynaptic membrane, thereby facilitating neurotransmitter release.
Synaptobrevin-2 is an 18 kDa protein that consists of several distinct domains:
- N-terminal domain: This region is proline-rich and contributes to the formation of the SNARE complex.
- Hydrophilic domain: Highly conserved, this domain is crucial for the protein’s function.
- Transmembrane anchor: This domain anchors the protein to the vesicle membrane.
- C-terminal domain: This region interacts with other SNARE proteins to mediate vesicle fusion.
The human recombinant form of Synaptobrevin-2 (1-94) is a truncated version of the protein, containing the first 94 amino acids. This recombinant protein is typically produced in Escherichia coli (E. coli) and is non-glycosylated .
Synaptobrevin-2 is predominantly found on the cytoplasmic surface of synaptic vesicles. It is involved in the formation of the SNARE complex with syntaxin-1 and SNAP-25, which are located on the target membrane. This complex is essential for the docking and fusion of synaptic vesicles, leading to the release of neurotransmitters into the synaptic cleft .
The human recombinant Synaptobrevin-2 (1-94) is widely used in laboratory research to study the mechanisms of synaptic vesicle fusion and neurotransmitter release. It is also used in the development of assays to screen for potential therapeutic agents that can modulate synaptic transmission.
The recombinant Synaptobrevin-2 (1-94) is produced in E. coli and purified using proprietary chromatographic techniques. The protein is fused to a 24 amino acid His-tag at the N-terminus, which facilitates its purification. The final product is a sterile, colorless solution containing phosphate-buffered saline (pH 7.4) and 10% glycerol .
The recombinant protein should be stored at 4°C if it will be used within 2-4 weeks. For longer storage periods, it is recommended to store the protein at -20°C with the addition of a carrier protein (0.1% HSA or BSA) to prevent degradation. Multiple freeze-thaw cycles should be avoided to maintain the protein’s stability .
