Recombinant Rat Nogo-A Fc Chimera Protein, CF

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

Recombinant Rat Nogo-A Fc Chimera 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 300 ng on a nitrocellulose-coated microplate.
• Source: Mouse myeloma cell line, NS0-derived rat Nogo-A protein

  Rat Nogo-A (Thr544 - Phe725) Accession # Q9JK11

  IEGRMD

  Human IgG 1 (Pro100 - Lys330)

  N-terminus

  C-terminus

• Accession #: Q9JK11
• N-terminal Sequence: Thr544
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Rtn4
• Purity: >95%, 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: 46.1 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: 75-85 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 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 Rat Nogo-A Fc Chimera 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). The amino acid segment 59 - 172 is reported to block fibroblast spreading, while the aa segment 544 - 725 blocks 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 aa 544 - 725 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 403:383.
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 (2445-NG)(2)

Publications using 2445-NG

• P Xiao, J Gu, W Xu, X Niu, J Zhang, J Li, Y Chen, Z Pei, J Zeng, S Xing RTN4/Nogo-A-S1PR2 negatively regulates angiogenesis and secondary neural repair through enhancing vascular autophagy in the thalamus after cerebral cortical infarction Autophagy, 2022-03-09;0(0):1-20. 2022-03-09 [PMID: 35263212] (In Vivo, Rat)
• Wright KT, El Masri W, Osman A, Roberts S, Chamberlain G, Ashton BA, Johnson WE Bone marrow stromal cells stimulate neurite outgrowth over neural proteoglycans (CSPG), myelin associated glycoprotein and Nogo-A. Biochem. Biophys. Res. Commun., 2007-01-10;354(2):559-66. 2007-01-10 [PMID: 17234155] (Bioassay, Chicken)

Bioinformatics

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