Recombinant Rat Nogo-A Fc Chimera (aa 1026-1090) Protein, CF

• Reactivity: Rt
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Rat Nogo-A Fc Chimera (aa 1026-1090) Protein, CF Summary

• Details of Functionality: Measured by its ability to inhibit neurite outgrowth of dissociated E13 chick embryonic dorsal root ganglia (DRG) neurons. Able to significantly inhibit neurite outgrowth when immobilized as a 3 µL droplet containing 200 ng on a nitrocellulose-coated microplate.
• Source: Spodoptera frugiperda, Sf 21 (baculovirus)-derived rat Nogo-A protein

  Rat Nogo-A (Arg1026-Leu1090) Accession #Q9JK11

  IEGRMDP

  Mouse IgG 2A (Glu98-Lys330)

  N-terminus

  C-terminus

• Accession #: Q9JK11
• N-terminal Sequence: Arg1026
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Rtn4
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 34.5 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.

Packaging, Storage & Formulations

• Storage: 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: >90%, 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 Rat Nogo-A Fc Chimera (aa 1026-1090) Protein, CF

• ASY;Nbla00271;Nbla10545;NI220/250;Nogo;NSP;NSP-CL;r;Reticulon-4;Rtn4;RTN4;RTN4-A;RTN4-B1;RTN4-B2;RTN4-C;RTN-X
• NI220
• NogoA
• Nogo-A
• RTN4
• RTN4A

Background

Rat Nogo-A is a member of the reticulon family of transmembrane proteins. This family is characterized by the presence of a nonsignal sequence-containing N-terminus, a topologically conserved approximately 200 amino acid (aa) C-terminus that contains two transmembrane domains and an ER-retention motif, and a punctate intracellular distribution within the ER that is reminescent of a reticulum (1, 2). Nogo-A in rat exists in four isoforms (3 - 5). The full length rat Nogo-A is 1163 aa in length and contains a 989 aa N-terminus, a 21 aa transmembrane segment, a 94 aa connecting “loop”, a second 21 aa transmembrane segment, and a 38 aa C-terminus. Three areas are of particular interest. One is a stretch of 66 aa within the 94 aa transmembrane connecting loop (SWISSPROT defines this region as being 94 aa in length while the original cloning papers identified it as being 66 aa in length). This segment is reported to bind to the GPI-linked Nogo receptor/p75 complex on axons and induce growth cone collapse (6 - 8). Two other areas in the N-terminus have also been discovered to have bioactivity (6, 9, 10). Amino acids 59 - 172 are reported to block fibroblast spreading, while aa 544 - 725 block neurite outgrowth and block fibroblast spreading (6, 10). The exact topology of Nogo-A is unclear. With two transmembrane segments, the N- and C-termini may be extracellular with the “loop” region intracellular, or the situation could be reversed (11, 12). Alternatively, the loop region and N-terminus may be on the same side of the membrane (6). Nogo-A is expressed in neurons, endothelial cells. oligodendrocytes, fibroblasts and myoblasts (10, 13, 14). Rat Nogo-A is 78% aa identical to human Nogo-A overall, with 98% aa identical in the loop region and 81% aa identity in the 544 - 725 aa segment.

1. Oertle, T. et al. (2003) FASEB J. 17:1238.
2. GrandPre, T. et al. (2000) Nature 403:439.
3. Chen, M.S. et al. (2000) Nature 403:434.
4. Morris, N.J. et al. (1999) Biochim. Biophys. Acta 1450:68.
5. Ito, T. and S.M. Schwartz (1999) GenBank Accession # Q9JK11.
6. Oertle, T. et al. (2003) J. Neurosci. 23:5393.
7. Fournier, A.E. et al. (2001) Nature 409:341.
8. Wang, K.C. et al. (2002) Nature 420:74.
9. Prinjha, R. et al. (2000) Nature 403:384.
10. Dodd, D.A. et al. (2005) J. Biol. Chem. 280:12494.
11. Huber, A.B. and M.E. Schwab (2000) Biol. Chem. 381:407.
12. Ng, C.E.L. and B.L. Tang (2002) J. Neurosci. Res. 67:559.
13. Wang, X. et al. (2002) J. Neurosci. 22:5505.
14. Acevedo, L. et al. (2004) Nat. Med. 10:382.

Publications for Nogo-A (3728-NG)(3)

Publications using 3728-NG

• Y Kawakami, Y Kurihara, Y Saito, Y Fujita, T Yamashita, K Takei The soluble form of LOTUS inhibits Nogo receptor-mediated signaling by interfering with the interaction between Nogo receptor type 1 and p75 neurotrophin receptor J. Neurosci., 2018-02-09;0(0):. 2018-02-09 [PMID: 29440387] (Bioassay, Mouse)
• Kurihara Y, Arie Y, Iketani M, Ito H, Nishiyama K, Sato Y, Nakamura F, Mizuki N, Goshima Y, Takei K The carboxyl-terminal region of Crtac1B/LOTUS acts as a functional domain in endogenous antagonism to Nogo receptor-1. Biochem. Biophys. Res. Commun., 2012-01-18;418(2):390-5. 2012-01-18 [PMID: 22281491] (Bioassay, Mouse)
• Matsushita H, Endo S, Kobayashi E, Sakamoto Y, Kobayashi K, Kitaguchi K, Kuroki K, Soderhall A, Maenaka K, Nakamura A, Strittmatter SM, Takai T Differential but competitive binding of Nogo protein and class i major histocompatibility complex (MHCI) to the PIR-B ectodomain provides an inhibition of cells. J. Biol. Chem., 2011-06-02;286(29):25739-47. 2011-06-02 [PMID: 21636572] (Bioassay, ICC, Surface Plasmon Resonance, Mouse)

Bioinformatics

• Gene Symbol: Rtn4
• Uniprot:
  • Q9JK11()