Recombinant Human Neurexin 1 beta Fc Chimera Protein, CF Summary
(100 μL/well) can bind Recombinant Human Neurexin 1 beta /NXRN1b Fc Chimera with an apparent Kd <4 nM.
|Human Neurexin 1 beta
Accession # NP_620072
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in sterile PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Background: Neurexin 1 beta/NXRN1b
The alpha and beta forms of Neurexins 1-3 are transmembrane neuronal glycoproteins which are transcribed from each of three NRXN genes that utilize alternate promoters. Like other Neurexins, the extracellular domain (ECD) of Neurexin 1 alpha contains six LNS domains interspersed with three EGF-like domains, while that of Neurexin 1 beta contains only the sixth LNS domain and no EGF-like domains (1 - 3). Mature human Neurexin 1 beta is a 70 kDa glycosylated protein with a 313 amino acid (aa) ECD and a 56 aa cytoplasmic domain that contains a motif for binding PDZ scaffolding proteins (2, 4, 5). Within comparable regions of the ECD, human Neurexin 1 beta shares 99% aa sequence identity with mouse and rat Neurexin 1 beta. It shares 42% and 68% aa sequence identity with the ECDs of human Neurexin 2 beta and 3 beta, respectively. Neurexin 1 beta isoforms are differentiated by a 30 aa insertion at alternative splice site 4 (SS4), numbered according to splice sites in the longer alpha Neurexins (4, 5). This recombinant protein does not include the SS4 insertion. Neurexin 1 beta is expressed presynaptically at neuronal contacts and interacts with postsynaptic Neuroligins 1-4. The presence of the SS4 insertion significantly weakens this interaction, particularly with Neuroligins 1 and 4 (6-12). Binding affinity is also dependent on the splicing pattern of the Neuroligin (7, 10, 11). Within the presynaptic terminal, Neurexin 1 beta is required for the recruitment of scaffolding proteins and synaptic vesicles (13). Its interaction with Neuroligins 1, 3, and 4 induces the development of glutamatergic postsynaptic terminals containing NMDA receptors, while its interaction with Neuroligin 2 promotes GABAergic postsynaptic development (10, 12, 14, 15). The presence of the SS4 insertion reduces the ability of Neurexin 1 beta to promote glutamatergic contacts but is required for the development of Neuroligin 2/GABAergic contact development (10, 12).
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Citations for Recombinant Human Neurexin 1 beta Fc Chimera Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 3
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The soluble neurexin-1&beta ectodomain causes calcium influx and augments dendritic outgrowth and synaptic transmission
Authors: KDB Wierda, TL Toft-Berte, CR Gøtzsche, E Pedersen, I Korshunova, J Nielsen, ML Bang, AB Kønig, S Owczarek, MD Gjørlund, M Schupp, E Bock, JB Sørensen
Sci Rep, 2020;10(1):18041.
Sample Types: Whole Cells
Computational geometry analysis of dendritic spines by structured illumination microscopy
Authors: Y Kashiwagi, T Higashi, K Obashi, Y Sato, NH Komiyama, SGN Grant, S Okabe
Nat Commun, 2019;10(1):1285.
Sample Types: Whole Cells
Amyloid-? Oligomers Interact with Neurexin and Diminish Neurexin-mediated Excitatory Presynaptic Organization
Authors: Y Naito, Y Tanabe, AK Lee, E Hamel, H Takahashi
Sci Rep, 2017;7(0):42548.
Sample Types: Protein
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