Recombinant Mouse Nogo Receptor Fc Chimera Protein, CF
Recombinant Mouse Nogo Receptor Fc Chimera Protein, CF Summary
Product Specifications
| Mouse Nogo Receptor (Cys27 - Ser447) Accession # Q99PI8 |
IEGRMD | Human IgG1 (Pro100 - Lys330) |
| N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
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.
1440-NG
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 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.
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Reconstitution Calculator
Background: Nogo Receptor/NgR
Nogo Receptor (NgR), also named reticulon 4 receptor, is a glycosylphosphoinositol (GPI)-anchored protein that belongs to the family of leucine-rich repeat (LRR) proteins (1). It is expressed predominantly in the central nervous systems in neurons and their axons. NgR plays an essential role in mediating axon growth inhibition induced by the structurally distinct myelin-derived proteins Nogo, myelin-associated glycoprotein (MAG), and myelin oligodendrocyte glycoprotein (Omgp) (2, 3). Human NgR cDNA encodes a 473 amino acid (aa) residue precursor with a 26 aa putative signal peptide, an LRR-type N-terminal region, eight LRR repeats, a cysteine-rich LRR-type C-terminal region, a GPI linkage domain and a 26 aa C-terminal propeptide that is removed in the mature form (1). All of the LRR domains within NgR are required for ligand binding and receptor oligomerization (4). NgR mediates its inhibitory actions by interacting with the p75 neurotrophin receptor (p75NTR), a tumor necrosis factor receptor superfamily (TNFRSF) member also known for modulating the activities of the Trk family of receptor tyrosine kinases, and for inducing apoptosis in neurons and oligodendrocytes (5). Upon ligand binding, NgR binds to and activates the p75NTR. The activated p75NTR then sequesters the Rho guanine dissociation inhibitor (Rho-GDI) away from Rho and allows Rho to change into the active GTP-bound state which can interact with signaling proteins to suppress axonal growth and regeneration (4). The truncated extracellular domain of NgR has been shown to bind the myelin-derived inhibitors and block inhibition of axon growth by myelin (6).
- Fournier, A.E. et al. (2001) Nature 409:341.
- GrandPre, T. et al. (2002) Nature 417:547.
- Wang, K.C. et al. (2002) Nature 420:74.
- Barton, W.A. et al. (2003) EMBO Journal 22:3291.
- Yamashita, T. and M. Tohyama (2003) Nature Neuroscience 6:461.
- Fournier, A.S. et al. (2002) J. Neurosci. 22:8876.
Citations for Recombinant Mouse Nogo Receptor 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.
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Limiting neuronal nogo receptor 1 signaling during experimental autoimmune encephalomyelitis (EAE) preserves axonal transport and abrogates inflammatory demyelination
Authors: JY Lee, MJ Kim, S Thomas, V Oorschot, G Ramm, P Mun Aui, Y Sekine, D Deliyanti, J Wilkinson-, B Niego, AR Harvey, P Theotokis, C McLean, SM Strittmatt, S Petratos
J. Neurosci., 2019-05-06;0(0):.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Synaptic function for the Nogo-66 receptor NgR1: regulation of dendritic spine morphology and activity-dependent synaptic strength.
Authors: Lee H, Raiker SJ, Venkatesh K, Geary R, Robak LA, Zhang Y, Yeh HH, Shrager P, Giger RJ
J. Neurosci., 2008-03-12;28(11):2753-65.
Species: Human, Mouse
Sample Types: Recombinant Protein
Applications: Binding Assay, Immunoprecipitation
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