Complexin-1/2 Antibody (B-9): sc-514321

Complexin-1/2 Antibody (B-9) is a mouse monoclonal IgG1 antibody that detects Complexin-1/2 in human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Complexin-1 and Complexin-2, also known as Synaphin-1 and Synaphin-2, are critical proteins located in the presynaptic terminals of both inhibitory and excitatory neurons, particularly in the hippocampus, where Complexin-1 and Complexin-2 play a vital role in neurotransmitter release. These proteins contain an α-helical middle domain of approximately 58 amino acids, which is essential for their function in promoting the formation of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) precomplexes by binding to syntaxin. This interaction is crucial for the regulation of calcium-dependent neurotransmitter release, as Complexins act at a late stage of this process, immediately following the calcium-triggering event and just before vesicle fusion. The absence of Complexins leads to a significant reduction in transmitter release efficiency, highlighting their importance in maintaining synaptic function. Notably, Complexin-2 has been implicated in long-term potentiation following tetanic stimulation, and progressive loss of Complexin-2 in the brains of mice with the Huntington disease mutation suggests a link between altered neurotransmitter release and the cognitive and motor dysfunctions associated with this neurodegenerative disorder. anti-Complexin-1/2 antibody (B-9) is therefore an invaluable tool for researchers studying synaptic transmission and related neurological conditions.

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Complexin-1/2 Antibody (B-9) References:

1. Complexin 1 knockout mice exhibit marked deficits in social behaviours but appear to be cognitively normal.  |  Drew, CJ., et al. 2007. Hum Mol Genet. 16: 2288-305. PMID: 17652102
2. Regulation of complexin 1 and complexin 2 in the developing human prefrontal cortex.  |  Salimi, K., et al. 2008. Synapse. 62: 273-82. PMID: 18240322
3. Complexin-1 enhances the on-rate of vesicle docking via simultaneous SNARE and membrane interactions.  |  Diao, J., et al. 2013. J Am Chem Soc. 135: 15274-7. PMID: 24083833
4. Complexin-1 and Foxp1 Expression Changes Are Novel Brain Effects of Alpha-Synuclein Pathology.  |  Gispert, S., et al. 2015. Mol Neurobiol. 52: 57-63. PMID: 25112678
5. Complexin induces a conformational change at the membrane-proximal C-terminal end of the SNARE complex.  |  Choi, UB., et al. 2016. Elife. 5: PMID: 27253060
6. C-terminal domain of mammalian complexin-1 localizes to highly curved membranes.  |  Gong, J., et al. 2016. Proc Natl Acad Sci U S A. 113: E7590-E7599. PMID: 27821736
7. Complexin Binding to Membranes and Acceptor t-SNAREs Explains Its Clamping Effect on Fusion.  |  Zdanowicz, R., et al. 2017. Biophys J. 113: 1235-1250. PMID: 28456331
8. Cell Types and Synapses Expressing the SNARE Complex Regulating Proteins Complexin 1 and Complexin 2 in Mammalian Retina.  |  Lux, UT., et al. 2021. Int J Mol Sci. 22: PMID: 34360929
9. Stabilization of the SNARE Core by Complexin-1 Facilitates Fusion Pore Expansion.  |  Pierson, J. and Shin, YK. 2021. Front Mol Biosci. 8: 805000. PMID: 34970598
10. VAMP2 regulates phase separation of α-synuclein.  |  Agarwal, A., et al. 2024. Nat Cell Biol. 26: 1296-1308. PMID: 38951707

The preferred Complexin-1/2 antibody is Complexin-1/2 Antibody (D-9): sc-365152.