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Complexin1/2 antibody SNARE binding domain - 122 102 K.O.

Complexins are nerve-terminal syntaxin binding proteins
Rabbit polyclonal antiserum
Cat. No.: 122 102
Amount: 200 µl
Price: $355.00
Cat. No. 122 102 200 µl antiserum, lyophilized. For reconstitution add 200 µl H2O, then aliquot and store at -20°C until use.
Antibodies should be stored at +4°C when still lyophilized. Do not freeze!
Applications
 
WB: 1 : 1000 up to 1 : 20000 (AP staining) gallery  
IP: yes (see remarks)
ICC: 1 : 200 up to 1 : 500 gallery  
IHC: yes (see remarks)
IHC-P: 1 : 200 gallery  
Immunogen Synthetic peptide corresponding to AA 45 to 81 from mouse Complexin2 (UniProt Id: P84086)
Reactivity Reacts with: human (O14810, Q6PUV4), rat (P63041, P84087), mouse (P63040, P84086), Guinea pig, cow, zebrafish, rabbit.
Other species not tested yet.
Specificity Recognizes complexin 1 and 2. K.O. validated PubMed: 11163241
Remarks

IP: Co-immunoprecipitates the SNARE complex.
Immunogen is located inside the mapped binding domain of complexin 2 to the SNARE complex (aa 41 - 91).
IHC: For optimal results, mild fixation (immersion fixation with 4% PFA for 15 min) according to Gierke et al. 2023 is recommended.

Data sheet 122_102.pdf

References for Complexin1/2 - 122 102

The proteomic landscape of synaptic diversity across brain regions and cell types.
van Oostrum M, Blok TM, Giandomenico SL, Tom Dieck S, Tushev G, Fürst N, Langer JD, Schuman EM
Cell (2023) 18624: 5411-5427.e23. 122 102 WB; tested species: mouse
Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins.
Wilhelm BG, Mandad S, Truckenbrodt S, Kröhnert K, Schäfer C, Rammner B, Koo SJ, Claßen GA, Krauss M, Haucke V, Urlaub H, et al.
Science (New York, N.Y.) (2014) 3446187: 1023-8. 122 102 WB
Involvement of complexin 2 in docking, locking and unlocking of different SNARE complexes during sperm capacitation and induced acrosomal exocytosis.
Tsai PS, Brewis IA, van Maaren J, Gadella BM
PloS one (2012) 73: e32603. 122 102 WB, ICC; tested species: mouse,pig
Complexin 2 modulates vesicle-associated membrane protein (VAMP) 2-regulated zymogen granule exocytosis in pancreatic acini.
Falkowski MA, Thomas DD, Groblewski GE
The Journal of biological chemistry (2010) 28546: 35558-66. 122 102 WB, ICC
Complexins regulate a late step in Ca2+-dependent neurotransmitter release.
Reim K, Mansour M, Varoqueaux F, McMahon HT, Südhof TC, Brose N, Rosenmund C
Cell (2001) 1041: 71-81. 122 102 WB; KO verified; tested species: mouse
Involvement of complexin 2 in docking, locking and unlocking of different SNARE complexes during sperm capacitation and induced acrosomal exocytosis.
Tsai PS, Brewis IA, van Maaren J, Gadella BM
PloS one (2012) 73: e32603. 122 102 WB, ICC; tested species: mouse,pig
Complexin 2 modulates vesicle-associated membrane protein (VAMP) 2-regulated zymogen granule exocytosis in pancreatic acini.
Falkowski MA, Thomas DD, Groblewski GE
The Journal of biological chemistry (2010) 28546: 35558-66. 122 102 WB, ICC
Cell Types and Synapses Expressing the SNARE Complex Regulating Proteins Complexin 1 and Complexin 2 in Mammalian Retina.
Lux UT, Ehrenberg J, Joachimsthaler A, Atorf J, Pircher B, Reim K, Kremers J, Gießl A, Brandstätter JH
International journal of molecular sciences (2021) 2215: . 122 102 IHC; KO verified; tested species: mouse
Immunocytochemical evidence for SNARE protein-dependent transmitter release from guinea pig horizontal cells.
Lee H, Brecha NC
The European journal of neuroscience (2010) 318: 1388-401. 122 102 IHC
Cat. No.: 122 102
Amount: 200 µl
Price: $355.00
The proteomic landscape of synaptic diversity across brain regions and cell types.
van Oostrum M, Blok TM, Giandomenico SL, Tom Dieck S, Tushev G, Fürst N, Langer JD, Schuman EM
Cell (2023) 18624: 5411-5427.e23. 122 102 WB; tested species: mouse
Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins.
Wilhelm BG, Mandad S, Truckenbrodt S, Kröhnert K, Schäfer C, Rammner B, Koo SJ, Claßen GA, Krauss M, Haucke V, Urlaub H, et al.
Science (New York, N.Y.) (2014) 3446187: 1023-8. 122 102 WB
Involvement of complexin 2 in docking, locking and unlocking of different SNARE complexes during sperm capacitation and induced acrosomal exocytosis.
Tsai PS, Brewis IA, van Maaren J, Gadella BM
PloS one (2012) 73: e32603. 122 102 WB, ICC; tested species: mouse,pig
Complexin 2 modulates vesicle-associated membrane protein (VAMP) 2-regulated zymogen granule exocytosis in pancreatic acini.
Falkowski MA, Thomas DD, Groblewski GE
The Journal of biological chemistry (2010) 28546: 35558-66. 122 102 WB, ICC
Complexins regulate a late step in Ca2+-dependent neurotransmitter release.
Reim K, Mansour M, Varoqueaux F, McMahon HT, Südhof TC, Brose N, Rosenmund C
Cell (2001) 1041: 71-81. 122 102 WB; KO verified; tested species: mouse
Involvement of complexin 2 in docking, locking and unlocking of different SNARE complexes during sperm capacitation and induced acrosomal exocytosis.
Tsai PS, Brewis IA, van Maaren J, Gadella BM
PloS one (2012) 73: e32603. 122 102 WB, ICC; tested species: mouse,pig
Complexin 2 modulates vesicle-associated membrane protein (VAMP) 2-regulated zymogen granule exocytosis in pancreatic acini.
Falkowski MA, Thomas DD, Groblewski GE
The Journal of biological chemistry (2010) 28546: 35558-66. 122 102 WB, ICC
Cell Types and Synapses Expressing the SNARE Complex Regulating Proteins Complexin 1 and Complexin 2 in Mammalian Retina.
Lux UT, Ehrenberg J, Joachimsthaler A, Atorf J, Pircher B, Reim K, Kremers J, Gießl A, Brandstätter JH
International journal of molecular sciences (2021) 2215: . 122 102 IHC; KO verified; tested species: mouse
Immunocytochemical evidence for SNARE protein-dependent transmitter release from guinea pig horizontal cells.
Lee H, Brecha NC
The European journal of neuroscience (2010) 318: 1388-401. 122 102 IHC
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.