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Recombinant Rat Nogo-A Fc Chimera Protein, CF

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Product Details

Summary
Reactivity RtSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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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 IgG1
(Pro100 - Lys330)
N-terminus C-terminus
Accession #
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
Publications
Read Publications using
2445-NG in the following applications:

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 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.

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Publications for Nogo-A (2445-NG)(2)

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Additional Nogo-A Products

Blogs on Nogo-A.

Nogo: A Promising Target for New Gene Therapies
Nogo is a neurite outgrowth inhibitor protein that plays an important role during central nervous system (CNS) development as well as in endoplasmic reticulum signaling regulation. Studies using Nogo antibodies have revealed Nogo proteins regulate ...  Read full blog post.

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Bioinformatics

Gene Symbol Rtn4
Uniprot