Recombinant Human Neuroligin 2/NLGN2 Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Neuroligin 2/NLGN2 is immobilized at 1.5 μg/mL,
Recombinant
Human Neurexin 1 beta /NXRN1b Fc Chimera (Catalog # 5268-NX)
binds with an apparent Kd <10 nM.
Source
Mouse myeloma cell line, NS0-derived human Neuroligin 2/NLGN2 protein Gln15-Ser660, with a C-terminal 6-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
72 kDa. 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 5645-NL 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 with Trehalose.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 400 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Neuroligin 2/NLGN2 Protein, CF
EC 3.1.1
EC 3.1.1.1
KIAA1366neuroligin-2
Neuroligin 2
NLGN2
Background
Neuroligin 2 (NLGN2) is one of several type I transmembrane Neuroligins that are expressed on neuronal postsynaptic densities. Neuroligins play an important role in synaptic development and function (1). Mature human Neuroligin 2 is a 105 kDa protein that consists of a 663 amino acid (aa) extracellular domain (ECD) with a catalytically inactive cholinesterase-like domain, a 21 aa transmembrane segment, and a 137 aa cytoplasmic tail (2, 3). Within the ECD, human Neuroligin 2 shares 98% aa sequence identity with mouse and rat Neuroligin 2. Alternate splicing generates an isoform with a 17 aa insertion at splice site A within the ECD (2). This recombinant protein does not contain the splice site A insert (-SS A). Neuroligin 2 is expressed on neurons in the brain and also on pancreatic beta cells where it facilitates insulin secretion (2, 4, 5). The -SS A isoform is uniformly expressed among inhibitory and excitatory synapses, while the +SS A isoform is enriched at inhibitory GABAergic synapses (4, 6, 7). Neuroligin 2 clusters at postsynaptic densities in association with other postsynaptic proteins including S-SCAM, PSD-95, gephyrin, and Neuroligin 3 (4, 8-10). Synaptic maturation is promoted by the binding of Neuroligin 2 with presynaptic Neurexins, and these interactions are restricted to particular combinations of isoforms of the binding partners (11-15). Neuroligin 2 interacts with the alpha and beta forms of Neurexin 1, 2, and 3 (14). Its -SS A and +SS A isoforms are bound equally well by Neurexin 1 beta isoforms (-SS4 or +SS4), although only the Neurexin 1 beta +SS4 isoform can induce development of Neuroligin 2-dependent GABAergic contacts (7, 15).
Sudhof, T.C. (2008) Nature 455:903.
Ichtchenko, K. et al. (1996) J. Biol. Chem. 271:2676.
Koehnke, J. et al. (2008) Proc. Natl. Acad. Sci. 105:1873.
Varoqueaux, F. et al. (2004) Eur. J. Cell Biol. 83:449.
Suckow, A.T. et al. (2008) Endocrinology 149:6006.
Graf, E.R. et al. (2004) Cell 119:1013.
Chih, B. et al. (2006) Neuron 51:171.
Sumita, K. et al. (2007) J. Neurochem. 100:154.
Irie, M. et al. (1997) Science 277:1511.
Budreck, E.C. and P. Scheiffele (2008) Eur. J. Neurosci. 26:1738.
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