Recombinant Human Neurexin 1 beta Fc Chimera Protein, CF Summary
Details of Functionality
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.
Source
Mouse myeloma cell line, NS0-derived human Neurexin 1 beta/NXRN1b protein
Human Neurexin 1 beta (Ala51-Ser363) Accession # NP_620072
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
59.9 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
85-95 kDa, reducing conditions
Publications
Read Publications using 5268-NX in the following applications:
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Neurexin 1 beta Fc Chimera Protein, CF
Hs.22998
Neurexin 1 beta
NXR1B
NXRN1b
PTHSL2
SCZD17
Background
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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Ichtchenko, K. et al. (1995) Cell 81:435.
Comoletti, D. et al. (2006) Biochemistry 45:12816.
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Arac, D. et al. (2007) Neuron 56:992.
Chih, B. et al. (2006) Neuron 51:171.
Boucard, A.A. et al. (2005) Neuron 48:229.
Graf, E.R. et al. (2006) J. Neurosci. 26:4256.
Dean, C. et al. (2003) Nat. Neurosci. 7:708.
Nam, C.I. and L. Chen (2005) Proc. Natl. Acad. Sci. 102:6137.
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