Recombinant Human Neurexin 1 beta Fc Chimera Protein, CF

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Recombinant Human Neurexin 1 beta Fc Chimera Protein, CF Summary

Product Specifications

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. Biotinylated recombinant rat NLGN-1v2 immobilized on a streptavidin-coated plate at 1 µg/mL
(100 μL/well) can bind Recombinant Human Neurexin 1 beta /NXRN1b Fc Chimera with an apparent Kd <4 nM.
Mouse myeloma cell line, NS0-derived human Neurexin 1 beta/NXRN1b protein
Human Neurexin 1 beta
Accession # NP_620072
N-terminus C-terminus
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
59.9 kDa (monomer)
85-95 kDa, reducing conditions

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Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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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).

  1. Craig, A.M. and Y. Kang (2007) Curr. Opin. Neurobiol. 17:43.
  2. Lise, M.-F. and A. El-Husseini (2006) Cell. Mol. Life Sci. 63:1833.
  3. Dean, C. and T. Dresbach (2006) Trends Neurosci. 29:21.
  4. Rowen, L. et al. (2002) Genomics 79:587.
  5. Ushkaryov, Y.A. et al. (1992) Science 257:50.
  6. Ichtchenko, K. et al. (1995) Cell 81:435.
  7. Comoletti, D. et al. (2006) Biochemistry 45:12816.
  8. Ichtchenko, K. et al. (1996) J. Biol. Chem. 271:2676.
  9. Arac, D. et al. (2007) Neuron 56:992.
  10. Chih, B. et al. (2006) Neuron 51:171.
  11. Boucard, A.A. et al. (2005) Neuron 48:229.
  12. Graf, E.R. et al. (2006) J. Neurosci. 26:4256.
  13. Dean, C. et al. (2003) Nat. Neurosci. 7:708.
  14. Nam, C.I. and L. Chen (2005) Proc. Natl. Acad. Sci. 102:6137.
  15. Graf, E.R. et al. (2004) Cell 119:1013.
Entrez Gene IDs
9378 (Human); 18189 (Mouse); 60391 (Rat)
Alternate Names
Hs.22998; Neurexin 1 beta; NXR1B; NXRN1b; PTHSL2; SCZD17

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.

3 Citations: Showing 1 - 3
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  1. 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.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  2. 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.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Neutralization
  3. 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.
    Species: Human
    Sample Types: Protein
    Applications: Immunoprecipitation


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