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Complexin1/2 antibody C-terminus - 122 003 K.O.

Complexins are nerve-terminal syntaxin binding proteins
Rabbit polyclonal purified antibody
Cat. No.: 122 003
Amount: 50 µg
Price: $455.00
Cat. No. 122 003 50 µg specific antibody, lyophilized. Affinity purified with the immunogen. Albumin and azide were added for stabilization. For reconstitution add 50 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C to -80°C until use.
Antibodies should be stored at +4°C when still lyophilized. Do not freeze!
Applications
 
WB: 1 : 1000 (AP staining) gallery  
IP: not tested yet
ICC: 1 : 500 gallery  
IHC: 1 : 200 up to 1 : 500 gallery  
IHC-P: not tested yet
Immunogen Synthetic peptide corresponding to AA 122 to 134 from human Complexin2 (UniProt Id: Q6PUV4)
Reactivity Reacts with: rat (P63041, P84087), mouse (P63040, P84086), human (O14810, Q6PUV4), cow, electric ray, rabbit.
Other species not tested yet.
Specificity Recognizes complexin 1 and 2. K.O. validated
Matching control protein/peptide 122-0P
Data sheet 122_003.pdf

References for Complexin1/2 - 122 003

Altered conformation of α-synuclein drives dysfunction of synaptic vesicles in a synaptosomal model of Parkinson's disease.
Fonseca-Ornelas L, Viennet T, Rovere M, Jiang H, Liu L, Nuber S, Ericsson M, Arthanari H, Selkoe DJ
Cell reports (2021) 361: 109333. 122 003 WB; tested species: mouse
Aberrant function and structure of retinal ribbon synapses in the absence of complexin 3 and complexin 4.
Reim K, Regus-Leidig H, Ammermüller J, El-Kordi A, Radyushkin K, Ehrenreich H, Brandstätter JH, Brose N
Journal of cell science (2009) 122Pt 9: 1352-61. 122 003 WB, IHC; tested species: mouse
Single synapse glutamate imaging reveals multiple levels of release mode regulation in mammalian synapses.
Farsi Z, Walde M, Klementowicz AE, Paraskevopoulou F, Woehler A
iScience (2021) 241: 101909. 122 003 ICC; tested species: rat
Aberrant function and structure of retinal ribbon synapses in the absence of complexin 3 and complexin 4.
Reim K, Regus-Leidig H, Ammermüller J, El-Kordi A, Radyushkin K, Ehrenreich H, Brandstätter JH, Brose N
Journal of cell science (2009) 122Pt 9: 1352-61. 122 003 WB, IHC; tested species: mouse
Cat. No.: 122 003
Amount: 50 µg
Price: $455.00
Altered conformation of α-synuclein drives dysfunction of synaptic vesicles in a synaptosomal model of Parkinson's disease.
Fonseca-Ornelas L, Viennet T, Rovere M, Jiang H, Liu L, Nuber S, Ericsson M, Arthanari H, Selkoe DJ
Cell reports (2021) 361: 109333. 122 003 WB; tested species: mouse
Aberrant function and structure of retinal ribbon synapses in the absence of complexin 3 and complexin 4.
Reim K, Regus-Leidig H, Ammermüller J, El-Kordi A, Radyushkin K, Ehrenreich H, Brandstätter JH, Brose N
Journal of cell science (2009) 122Pt 9: 1352-61. 122 003 WB, IHC; tested species: mouse
Single synapse glutamate imaging reveals multiple levels of release mode regulation in mammalian synapses.
Farsi Z, Walde M, Klementowicz AE, Paraskevopoulou F, Woehler A
iScience (2021) 241: 101909. 122 003 ICC; tested species: rat
Aberrant function and structure of retinal ribbon synapses in the absence of complexin 3 and complexin 4.
Reim K, Regus-Leidig H, Ammermüller J, El-Kordi A, Radyushkin K, Ehrenreich H, Brandstätter JH, Brose N
Journal of cell science (2009) 122Pt 9: 1352-61. 122 003 WB, IHC; tested species: mouse
Background

Complexins are enriched in neurons where they colocalize with syntaxin 1 and SNAP 25. In addition, complexin 2, also referred to as synaphin 1, 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 (synaphin 2) and 2. They have similar biochemical binding properties and are farnesylated at their C-terminus.