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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
Loss of the parkinsonism-associated protein FBXO7 in glutamatergic forebrain neurons in mice leads to abnormal motor behavior and synaptic defects.
Wang J, Joseph S, Vingill S, Dere E, Tatenhorst L, Ronnenberg A, Lingor P, Preisinger C, Ehrenreich H, Schulz JB, Stegmüller J, et al.
Journal of neurochemistry (2023) : . 122 003 IHC; 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
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
Loss of the parkinsonism-associated protein FBXO7 in glutamatergic forebrain neurons in mice leads to abnormal motor behavior and synaptic defects.
Wang J, Joseph S, Vingill S, Dere E, Tatenhorst L, Ronnenberg A, Lingor P, Preisinger C, Ehrenreich H, Schulz JB, Stegmüller J, et al.
Journal of neurochemistry (2023) : . 122 003 IHC; 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
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.