Invitrogen™ CPLX1/2 Polyclonal Antibody

Complexins (1 through 4) are small cytosolic proteins that bind tightly to a complex of SNARE proteins to regulate synaptic vesicle membrane fusion via its interaction withsynaptotagmin. Complexins activate the quick release of neurotransmitters, triggered by calcium release. They also regulate the spontaneous release of neurotransmitters. Complexins are evolutionarily conserved in mammals, Drosophila, and Caenorhabditis elegans. They are divided into four structural domains: flexible N- and C-terminal domains, an accessory domain, and a central alpha-helical domain. The N-terminal domain plays a role in activation of fast synchronous release in murine neurons and in isolated chromaffin cells. The C-terminal domain binds to phospholipids and is important for regulating spontaneous release in neuronal cultures and suppressing Ca2+-independent fusion in vitro. The accessory domain is necessary for regulating spontaneous release and the central domain is required for all functions.