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Neurexin 1/2/3 - 175 003

A receptor-like neuronal cell-surface protein
Polyclonal rabbit purified antibody
Cat. No.: 175 003
Amount: 50 µg
Price: $370.00
Cat. No. 175 003 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.
Applications WB: 1 : 500 up to 1 : 1000 (AP staining) (see remarks) gallery  
IP: not tested yet
ICC: not recommended
IHC: not tested yet
IHC-P/FFPE: not tested yet
Immunogen Recombinant protein corresponding to AA 1459 to 1514 and 1657 to 1712 and 1524 to 1578 from rat Neurexin1/2/3
Reactivity Reacts with: rat (Q63372, Q63376, Q07310), mouse (Q9CS84, E9PUM9, Q8C985).
Other species not tested yet.
Specificity Due to the homology of the cytoplasmic tails of α- and β-neurexins 1, 2 and 3, this antiserum detects all isoforms and their corresponding splice-variants. K.O. PubMed: 30104341
Remarks

WB: Non-boiled samples yield stronger signals.

Data sheet 175_003.pdf

References for Neurexin 1/2/3 - 175 003

α-Neurexins Together with α2δ-1 Auxiliary Subunits Regulate Ca2+ Influx through Cav2.1 Channels.
Brockhaus J, Schreitmüller M, Repetto D, Klatt O, Reissner C, Elmslie K, Heine M, Missler M
The Journal of neuroscience : the official journal of the Society for Neuroscience (2018) 3838: 8277-8294. 175 003 WB; KO verified; tested species: mouse
A novel synaptic junction preparation for the identification and characterization of cleft proteins.
Burch A, Tao-Cheng JH, Dosemeci A
PloS one (2017) 123: e0174895. 175 003 WB, EM; tested species: rat
Physical Interactions and Functional Relationships of Neuroligin 2 and Midbrain Serotonin Transporters.
Ye R, Quinlan MA, Iwamoto H, Wu HH, Green NH, Jetter CS, McMahon DG, Veestra-VanderWeele J, Levitt P, Blakely RD
Frontiers in synaptic neuroscience (2015) 7: 20. 175 003 WB; tested species: mouse
Processing of the synaptic cell adhesion molecule neurexin-3beta by Alzheimer disease alpha- and gamma-secretases.
Bot N, Schweizer C, Ben Halima S, Fraering PC
The Journal of biological chemistry (2011) 2864: 2762-73. 175 003 WB
Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn.
Lim SH, Kwon SK, Lee MK, Moon J, Jeong DG, Park E, Kim SJ, Park BC, Lee SC, Ryu SE, Yu DY, et al.
The EMBO journal (2009) 2822: 3564-78. 175 003 WB
A novel synaptic junction preparation for the identification and characterization of cleft proteins.
Burch A, Tao-Cheng JH, Dosemeci A
PloS one (2017) 123: e0174895. 175 003 WB, EM; tested species: rat
Cat. No.: 175 003
Quantity: 50 µg
Price: $370.00
α-Neurexins Together with α2δ-1 Auxiliary Subunits Regulate Ca2+ Influx through Cav2.1 Channels.
Brockhaus J, Schreitmüller M, Repetto D, Klatt O, Reissner C, Elmslie K, Heine M, Missler M
The Journal of neuroscience : the official journal of the Society for Neuroscience (2018) 3838: 8277-8294. 175 003 WB; KO verified; tested species: mouse
A novel synaptic junction preparation for the identification and characterization of cleft proteins.
Burch A, Tao-Cheng JH, Dosemeci A
PloS one (2017) 123: e0174895. 175 003 WB, EM; tested species: rat
Physical Interactions and Functional Relationships of Neuroligin 2 and Midbrain Serotonin Transporters.
Ye R, Quinlan MA, Iwamoto H, Wu HH, Green NH, Jetter CS, McMahon DG, Veestra-VanderWeele J, Levitt P, Blakely RD
Frontiers in synaptic neuroscience (2015) 7: 20. 175 003 WB; tested species: mouse
Processing of the synaptic cell adhesion molecule neurexin-3beta by Alzheimer disease alpha- and gamma-secretases.
Bot N, Schweizer C, Ben Halima S, Fraering PC
The Journal of biological chemistry (2011) 2864: 2762-73. 175 003 WB
Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn.
Lim SH, Kwon SK, Lee MK, Moon J, Jeong DG, Park E, Kim SJ, Park BC, Lee SC, Ryu SE, Yu DY, et al.
The EMBO journal (2009) 2822: 3564-78. 175 003 WB
A novel synaptic junction preparation for the identification and characterization of cleft proteins.
Burch A, Tao-Cheng JH, Dosemeci A
PloS one (2017) 123: e0174895. 175 003 WB, EM; tested species: rat
Background
α- and β-neurexins are single pass transmembrane proteins with a short cytoplasmic C-terminus and a long extracellular N-terminal part. In α-neurexins the extracellular sequence is substantially longer than in β-neurexins. Alternative splicing of the N-terminal part even confers more complexity to this protein family suggesting distinct binding partners for the extracellular regions. In contrast, the C-termini are highly conserved in the different isoforms and splice-variants and they share overlapping cytosolic binding partners.
Neurexins are receptor like molecules that form heterologous cell contacts with post-synaptic cell surface proteins at synaptic connections (e.g. β-neurexins with neuroligins). They also serve as receptors for the black widow toxin α-latrotoxin which induces neurotransmitter release.