CPLX1 Human

Complexin-1 is composed of a central α-helical domain flanked by unstructured amino- and carboxy-terminal domains . This structure allows it to bind to t-SNAREs with low affinity and to assembled SNARE complexes with high affinity . The protein is primarily expressed in neuronal cells, where it regulates both evoked and spontaneous exocytosis .

Complexin-1 has a dual role in neurotransmitter release. It acts as a positive regulator of transmitter release at hippocampal glutamatergic synapses by enhancing Ca2±triggered fast neurotransmitter release . However, it also inhibits SNARE-mediated liposome and cell fusions in vitro, leading to the hypothesis that it functions as a fusion clamp during synaptic exocytosis .

Recombinant Human Complexin-1 is produced using Escherichia coli (E. coli) expression systems. The protein is expressed with an N-terminal His-tag and purified using conventional chromatography techniques . The recombinant protein is typically greater than 90% pure, as determined by SDS-PAGE, and has a theoretical molecular weight of approximately 17.1 kDa .

Recombinant Complexin-1 is used extensively in research to study synaptic vesicle exocytosis and neurotransmitter release mechanisms. It is also employed in various biochemical assays to investigate the interactions between SNARE proteins and other regulatory factors involved in synaptic transmission .

For optimal stability, recombinant Complexin-1 should be stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid repeated freeze-thaw cycles to maintain the protein’s integrity .