>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
Binding Activity
Theoretical MW
71.8 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
95-105 kDa, reducing conditions
Publications
Read Publications using 1208-NG in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC 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 100 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 Nogo Receptor Fc Chimera Protein, CF
NgR
NgR1
Nogo R
Nogo receptor
Nogo-66 receptor
NogoR
NOGORUNQ330/PRO526
reticulon 4 receptor
reticulon-4 receptor
RTN4R
Background
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 residues (aa) 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 (p75 NTR ), 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 p75 NTR . The activated p75 NTR 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.
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