Recombinant Human Neuroligin 1v2 (-ssB)/NLGN1v2 (-ssB), CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When recombinant human Neuroligin 1 is immobilized at 5.0 μg/mL, recombinant human Neurexin 1 beta Fc Chimera (Catalog # 5268-NX) binds with an apparent KD < 10 nM. |
Source |
Mouse myeloma cell line, NS0-derived human Neuroligin 1/NLGN1 protein Gln46-Ser677, Deletion: aa 279-287, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
No results obtained: Gln46 predicted
|
Structure / Form |
Noncovalently-linked homodimer
|
Protein/Peptide Type |
Recombinant Proteins |
Gene |
NLGN1 |
Purity |
>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 |
|
Theoretical MW |
70.3 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 |
90-100 kDa, reducing conditions |
Packaging, Storage & Formulations
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.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions |
Reconstitute at 200 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 1v2 (-ssB)/NLGN1v2 (-ssB), CF
Background
Neuroligin 1 (NLGN1 or NL1) is one of several type I transmembrane Neuroligin proteins that play an important role in synaptic development (1). Mature human Neuroligin 1 is an N- and O-glycosylated 120 kDa molecule that consists of a 649 amino acid (aa) extracellular domain (ECD) with a catalytically inactive cholinesterase-like domain, a 21 aa transmembrane segment, and a 125 aa cytoplasmic tail (2). In rat, insertion of 20 aa at splice site A and/or 9 aa at splice site B within the ECD results in NLGN1A, NLGN1B, or NLGN1AB isoforms while the NLGN1(-) isoform has neither insertion (3). This recombinant protein lacks both the splice site A and splice site B inserts and corresponds to the human equivalent of rat NLGN1(-). A protein lacking both insertions has also been predicted in chimpanzee (Accession # XP_001166442). Within the ECD, human NLGN1(-) shares 99% aa sequence identity with comparable regions of mouse and rat Neuroligin 1, respectively. Neuroligin 1 expression is restricted to postsynaptic nerve terminal membranes where it associates into dimers and tetramers (5 ‑ 7). NLGN1B and NLGN1AB are enriched at excitatory (glutamatergic) contacts, whereas NLGN1A is enriched at inhibitory (GABAergic) contacts and NLGN1(-) is expressed at both (3). The interaction of Neuroligin 1 with presynaptic membrane Neurexins promotes the maturation of presynaptic as well as postsynaptic structures (3, 4, 8 ‑ 11). Neuroligin 1 isoforms are selective in which Neurexin isoforms they bind: NLGN1B and NLGN1AB preferentially interact with Neurexin 1 beta lacking the splice site 4 insert, while NLGN1A and NLGN1(-) bind Neurexin 1 alpha and Neurexin 1 beta irrespective of the SS4 insert (12). Neurexin 1 beta (-SS4) additionally binds to LRRTM2 to trigger a second mechanism that promotes excitatory synapse development (13, 14). Neuroligin 1 mediated synaptogenesis is also enhanced by its direct binding to Thrombospondin 1 (15).
- Sudhof, T.C. (2008) Nature 455:903.
- Ichtchenko, K. et al. (1995) Cell 81:435.
- Chih, B. et al. (2006) Neuron 51:171.
- Dean, C. et al. (2003) Nat. Neurosci. 7:708.
- Comoletti, D. et al. (2006) Biochemistry 45:12816.
- Berninghausen, O. et al. (2007) J. Neurochem. 103:1855.
- Song, J.-Y. et al. (1999) Proc. Natl. Acad. Sci. 96:1100.
- Wittenmayer, N. et al. (2009) Proc. Natl. Acad. Sci. 106:13564.
- Jung, S.-Y. et al. (2010) Proc. Natl. Acad. Sci. 107:4710.
- Chubykin, A.A. et al. (2007) Neuron 54:919.
- Chih, B. et al. (2005) Science 307:1324.
- Boucard, A.A. et al. (2005) Neuron 48:229.
- Siddiqui, T.J. et al. (2010) J. Neurosci. 30:7495.
- Ko, J. et al. (2009) Neuron 64:791.
- Xu, J. et al. (2010) Nat. Neurosci. 13:22.
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