Recombinant Proteins
Product List
VAMP1 Human
Synaptobrevin-1 Human Recombinant
VAMP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (1-91) and having a molecular mass of 11.9 kDa. The VAMP-1 contains 20 amino acids His-Tag fused at N-terminus and purified by standard chromatography techniques.
VAMP2 Human
Synaptobrevin-2 Human Recombinant
VAMP2 Human, (1-94)
Synaptobrevin-2 Human Recombinant, (1-94)
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.
VAMP2 Mouse
Synaptobrevin-2 Recombinant Mouse
VAMP2 Mouse 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.
VAMP3 Human
Synaptobrevin-3 Human Recombinant
VAMP4 Human
Vesicle-associated membrane protein 4 Human Recombinant
VAMP4 is fused to an 8 amino acids His Tag at C-terminus and purified by proprietary chromatographic techniques.
VAMP5 Human
Vesicle-associated membrane protein 5 Human Recombinant
VAMP5 is fused to 37 amino acids His Tag at N-terminus and purified by proprietary chromatographic techniques.
VAMP7 Human
Vesicle-Associated Membrane Protein 7 Human Recombinant
VAMP7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
VAMP8 Human
Endobrevin Human Recombinant
VAPA Human
VAMP Associated Protein A 33kDa Human Recombinant
Introduction
Synaptobrevin, also known as vesicle-associated membrane protein (VAMP), is a small integral membrane protein found in secretory vesicles. It is a crucial component of the SNARE (soluble NSF attachment protein receptor) complex, which is essential for the fusion of vesicles with target membranes during exocytosis . Synaptobrevin is classified as an R-SNARE due to the presence of an arginine residue at a specific location within its primary sequence . In the V/T nomenclature, it is classified as a V-SNARE, indicating its localization to vesicles .
Synaptobrevin is a protein with a molecular weight of approximately 18 kilodaltons (kDa) . It is predominantly expressed in neurons, where it is localized to synaptic vesicles . The protein is also found in other secretory cells, such as endocrine cells . Synaptobrevin’s expression is tightly regulated, and it is distributed throughout the nervous system, with high concentrations in the brain .
The primary function of synaptobrevin is to mediate the fusion of synaptic vesicles with the presynaptic membrane, facilitating the release of neurotransmitters into the synaptic cleft . This process is critical for synaptic transmission and communication between neurons . Synaptobrevin also plays a role in the immune response by participating in the exocytosis of cytotoxic granules from immune cells . Additionally, it is involved in pathogen recognition and the immune response to infections .
Synaptobrevin interacts with other SNARE proteins, such as syntaxin and SNAP-25, to form the SNARE complex . This complex undergoes a conformational change that brings the vesicle and target membranes into close proximity, allowing them to fuse . Synaptobrevin’s binding partners include synaptophysin, which regulates its trafficking and assembly into the SNARE complex . The downstream signaling cascades initiated by synaptobrevin-mediated vesicle fusion are essential for neurotransmitter release and synaptic plasticity .
The expression and activity of synaptobrevin are regulated at multiple levels. Transcriptional regulation involves various transcription factors that control the gene expression of synaptobrevin . Post-translational modifications, such as phosphorylation and ubiquitination, also play a role in modulating synaptobrevin’s function and stability . Additionally, synaptobrevin is subject to degradation by specific proteases, such as tetanospasmin and botulinum toxin, which cleave the protein and inhibit its function .
Synaptobrevin has several applications in biomedical research and clinical practice. It is used as a marker for synaptic vesicles in studies of synaptic transmission and neurodegenerative diseases . Synaptobrevin’s role in exocytosis makes it a target for therapeutic strategies aimed at modulating neurotransmitter release in conditions such as epilepsy and depression . Additionally, synaptobrevin-based diagnostic tools are being developed to detect and monitor neurological disorders .
Throughout the life cycle, synaptobrevin plays a critical role in the development, function, and maintenance of the nervous system . During development, synaptobrevin is involved in the formation and maturation of synapses . In adulthood, it is essential for synaptic plasticity and memory formation . In aging and disease, alterations in synaptobrevin expression and function are associated with neurodegenerative conditions, such as Alzheimer’s disease and Parkinson’s disease .
