Complexin 2: Rat, mouse, human – 13/14 amino acid residues identical.
- Western blot analysis of mouse (lanes 1 and 3) and rat (lanes 2 and 4) brain lysates:1,2. Anti-CPLX1/2 Antibody (#ANR-011), (1:200).
3,4. Anti-CPLX1/2 Antibody, preincubated with CPLX1/2 Blocking Peptide (#BLP-NR011).
- Western blot analysis of human SH-SY5Y neuroblastoma cell line lysate:1. Anti-CPLX1/2 Antibody (#ANR-011), (1:200).
2. Anti-CPLX1/2 Antibody, preincubated with CPLX1/2 Blocking Peptide (#BLP-NR011).
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 with synaptotagmin. Complexins activate the quick release of neurotransmitters, triggered by calcium release. They also regulate the “spontaneous release” of neurotransmitters1-3.
Complexins are evolutionarily conserved in mammals, Drosophila, and Caenorhabditis elegans1,2. They are divided into four structural domains: flexible N- and C-terminal domains, an accessory domain, and a central α-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 functions1,2.
Species reactivity key:
Anti-CPLX1/2 Antibody (#ANR-011) is an antibody directed against epitopes of rat Complexin 1 and Complexin 2. The antibody can be used in western blot analysis. It has been designed to recognize both Complexin 1 and Complexin 2 from human, rat, and mouse samples.