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Neurexin 1 - 175 103

A receptor-like neuronal cell-surface protein
Polyclonal rabbit purified antibody
Cat. No.: 175 103
Amount: 50 µg
Price: $370.00
Cat. No. 175 103 50 µg specific antibody, lyophilized. Affinity purified with the immunogen. Albumin was 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 recommended
IHC-P/FFPE: not tested yet
Immunogen Recombinant protein corresponding to AA 1328 to 1421 from rat Neurexin1 (UniProt Id: Q63372)
Reactivity Reacts with: rat (Q63372), mouse (Q9CS84).
Other species not tested yet.
Specificity Specific for neurexin 1. The epitope is present in α- and β-neurexin 1.
Remarks

WB: Non-boiled samples yield stronger signals.

Data sheet 175_103.pdf

References for Neurexin 1 - 175 103

Deorphanizing FAM19A proteins as pan-neurexin ligands with an unusual biosynthetic binding mechanism.
Khalaj AJ, Sterky FH, Sclip A, Schwenk J, Brunger AT, Fakler B, Südhof TC
The Journal of cell biology (2020) 2199: . 175 103 WB; tested species: mouse
A rare autism-associated MINT2/APBA2 mutation disrupts neurexin trafficking and synaptic function.
Lin AY, Henry S, Reissner C, Neupert C, Kenny C, Missler M, Beffert U, Ho A
Scientific reports (2019) 91: 6024. 175 103 WB; tested species: mouse
Cat. No.: 175 103
Quantity: 50 µg
Price: $370.00
Deorphanizing FAM19A proteins as pan-neurexin ligands with an unusual biosynthetic binding mechanism.
Khalaj AJ, Sterky FH, Sclip A, Schwenk J, Brunger AT, Fakler B, Südhof TC
The Journal of cell biology (2020) 2199: . 175 103 WB; tested species: mouse
A rare autism-associated MINT2/APBA2 mutation disrupts neurexin trafficking and synaptic function.
Lin AY, Henry S, Reissner C, Neupert C, Kenny C, Missler M, Beffert U, Ho A
Scientific reports (2019) 91: 6024. 175 103 WB; tested species: mouse
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.