The human recombinant Syntaxin-1A (1-265 a.a) is a full-length protein comprising 265 amino acids. It is expressed in Escherichia coli and has a purity greater than 95%, making it suitable for various biochemical applications such as SDS-PAGE . The protein is also known by several alternative names, including Neuron-specific antigen HPC-1, STX1A, and STX1 .
Syntaxin-1A is primarily found in the brain and is essential for synaptic vesicle exocytosis. It interacts with other SNARE proteins, such as SNAP-25 and VAMP (vesicle-associated membrane protein), to form a SNARE complex. This complex brings the vesicle and plasma membranes close together, facilitating their fusion and the subsequent release of neurotransmitters .
The protein’s structure includes a transmembrane domain that anchors it to the plasma membrane and a cytoplasmic domain that interacts with other SNARE proteins. The interaction between Syntaxin-1A and its partners is highly regulated and crucial for the precise timing of neurotransmitter release, which is essential for proper neuronal communication .
Recombinant Syntaxin-1A (1-265 a.a) is widely used in research to study the mechanisms of synaptic transmission and the role of SNARE proteins in vesicle fusion. It is also used in various assays to investigate the interactions between SNARE proteins and other regulatory factors involved in neurotransmitter release .
Understanding the function and regulation of Syntaxin-1A is important for elucidating the molecular basis of synaptic transmission and for developing potential therapeutic strategies for neurological disorders that involve synaptic dysfunction.