VAMP1 Human
Greater than 95.0% as determined by SDS-PAGE.
Description
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.
Product Specs
MGSSHHHHHH SSGLVPRGSH MSAPAQPPAE GTEGTAPGGG PPGPPPNMTS NRRLQQTQAQVEEVVDIIRV NVDKVLERDQ KLSELDDRAD ALQAGASQFE SSAAKLKRKY W.
Product Science Overview
Synaptobrevin-1, also known as VAMP1 (Vesicle-Associated Membrane Protein 1), is a crucial protein involved in the process of synaptic vesicle fusion and neurotransmitter release in neurons. It is a member of the SNARE (Soluble NSF Attachment Protein Receptor) protein family, which plays a vital role in the fusion of vesicles with target membranes, a process essential for neurotransmission.
Synaptobrevin-1 is a small integral membrane protein with a molecular weight of approximately 18 kilodaltons (kDa). It is characterized by a single transmembrane domain and a cytoplasmic domain that participates in the formation of the SNARE complex. The SNARE complex is composed of four α-helices: one contributed by synaptobrevin, one by syntaxin, and two by SNAP-25 .
The primary function of synaptobrevin-1 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 the transmission of signals between neurons. Synaptobrevin-1, along with other SNARE proteins, forms a tight complex that brings the vesicle and target membranes into close proximity, allowing them to fuse .
Synaptobrevin-1 is essential for the proper functioning of the nervous system. It is involved in the regulated release of neurotransmitters, which is crucial for various physiological processes, including memory consolidation, mood regulation, and overall neuronal communication. Disruptions in synaptobrevin-1 function can lead to neurological disorders such as epilepsy, depression, and neurodegeneration .
Synaptobrevin-1 is a target for various bacterial toxins, including tetanospasmin (produced by Clostridium tetani) and botulinum toxin (produced by Clostridium botulinum). These toxins cleave synaptobrevin-1, inhibiting neurotransmitter release and leading to conditions such as tetanus and botulism .
Recombinant synaptobrevin-1 is produced using genetic engineering techniques, where the gene encoding synaptobrevin-1 is inserted into an expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications to study the mechanisms of synaptic vesicle fusion and neurotransmitter release.
