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

Catalog # Availability Size / Price Qty
3728-NG-050
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Rat Nogo-A Fc Chimera (aa 1026-1090) Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
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 IgG2A
(Glu98-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Analysis
Arg1026
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
34.5 kDa (monomer)

Product Datasheets

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3728-NG

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.

3728-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.
  • 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.
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Background: Nogo-A

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.

References
  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.
Long Name
Reticulon 4A
Entrez Gene IDs
57142 (Human); 68585 (Mouse); 83765 (Rat)
Alternate Names
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

Citations for Recombinant Rat Nogo-A Fc Chimera (aa 1026-1090) 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.

3 Citations: Showing 1 - 3
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  1. The soluble form of LOTUS inhibits Nogo receptor-mediated signaling by interfering with the interaction between Nogo receptor type 1 and p75 neurotrophin receptor
    Authors: Y Kawakami, Y Kurihara, Y Saito, Y Fujita, T Yamashita, K Takei
    J. Neurosci., 2018-02-09;0(0):.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  2. The carboxyl-terminal region of Crtac1B/LOTUS acts as a functional domain in endogenous antagonism to Nogo receptor-1.
    Authors: Kurihara Y, Arie Y, Iketani M, Ito H, Nishiyama K, Sato Y, Nakamura F, Mizuki N, Goshima Y, Takei K
    Biochem. Biophys. Res. Commun., 2012-01-18;418(2):390-5.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Differential but competitive binding of Nogo protein and class i major histocompatibility complex (MHCI) to the PIR-B ectodomain provides an inhibition of cells.
    Authors: Matsushita H, Endo S, Kobayashi E, Sakamoto Y, Kobayashi K, Kitaguchi K, Kuroki K, Soderhall A, Maenaka K, Nakamura A, Strittmatter SM, Takai T
    J. Biol. Chem., 2011-06-02;286(29):25739-47.
    Species: Mouse
    Sample Types: Protein, Whole Cells
    Applications: Bioassay, ICC, Surface Plasmon Resonance

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