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Complexin 3 - 122 311

A nerve-terminal syntaxin binding protein in retinal ribbon synapses
Monoclonal mouse purified IgG
Cat. No.: 122 311
Amount: 100 µg
Price: $415.00
Cat. No. 122 311 100 µg purified IgG, lyophilized. For reconstitution add 100 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C to -80°C until use.
Applications WB: 1 : 1000 (ECL detection) gallery  
IP: not tested yet
ICC: not tested yet
IHC: 1 : 500 gallery  
IHC-P/FFPE: 1 : 200 gallery  
Clone 294C2
Subtype IgG1 (κ light chain)
Immunogen Recombinant protein corresponding to AA 1 to 158 from mouse Complexin3 (UniProt Id: Q8R1B5)
Reactivity Reacts with: rat (D4ABY0), mouse (Q8R1B5).
Other species not tested yet.
Specificity Specific for complexin 3, no cross reaction to other complexins. K.O.
Data sheet 122_311.pdf

References for Complexin 3 - 122 311

Functional roles of complexin in neurotransmitter release at ribbon synapses of mouse retinal bipolar neurons.
Vaithianathan T, Henry D, Akmentin W, Matthews G
The Journal of neuroscience : the official journal of the Society for Neuroscience (2015) 359: 4065-70. 122 311 ICC
Molecular diversity of early-born subplate neurons.
Hoerder-Suabedissen A, Molnár Z
Cerebral cortex (New York, N.Y. : 1991) (2013) 236: 1473-83. 122 311 IHC; tested species: mouse
Cat. No.: 122 311
Quantity: 100 µg
Price: $415.00
Functional roles of complexin in neurotransmitter release at ribbon synapses of mouse retinal bipolar neurons.
Vaithianathan T, Henry D, Akmentin W, Matthews G
The Journal of neuroscience : the official journal of the Society for Neuroscience (2015) 359: 4065-70. 122 311 ICC
Molecular diversity of early-born subplate neurons.
Hoerder-Suabedissen A, Molnár Z
Cerebral cortex (New York, N.Y. : 1991) (2013) 236: 1473-83. 122 311 IHC; tested species: mouse
Background

Complexins are enriched in neurons where they colocalize with syntaxin 1 and SNAP 25. In addition, complexin 2 is expressed ubiquitously at low levels. Complexins bind weakly to syntaxin 1 alone and not at all to synaptobrevin and SNAP 25, but strongly to the SNAP receptor-core complex composed of these three molecules. They compete with α-SNAP for binding to the core complex but not with other interacting molecules, suggesting that complexins regulate the sequential interactions of α-SNAP and synaptotagmins with the SNAP receptor during exocytosis.
In retinal ribbon synapses complexin 3 and complexin 4 functionally replace complexin 1 and 2. They have similar biochemical binding properties and are farnesylated at their C-terminus.