Recombinant Human NrCAM Fc Chimera Protein, CF

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Recombinant Human NrCAM Fc Chimera Protein, CF Summary

Product Specifications

>95%, 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.
Measured by the ability of the immobilized protein to support the adhesion of Y‑79 human retinoblastoma cells. The ED50 for this effect is 0.8-4 μg/mL.
Mouse myeloma cell line, NS0-derived human NrCAM protein
Human NrCAM
Leu30-Asn600 (Ala526Pro)
Accession # Q14CA1
N-terminus C-terminus
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
90 kDa (monomer)
120-130 kDa, reducing conditions

Product Datasheets

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.


Formulation Lyophilized from a 0.2 μm filtered solution in MES and NaCl.
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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Reconstitution Calculator

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Background: NrCAM

NrCAM, also known as Bravo, belongs to the L1 family of cell adhesion molecules which also includes L1CAM, Neurofascin, and CHL-1/L1CAM-2 (1). These molecules are type I transmembrane proteins that have 6 Ig-like domains and 4-5 fibronectin type III-like domains in their extracellular domain. L1 family cell adhesion molecules are expressed primarily in the nervous system where they share overlapping functions in controlling axonal growth and guidance (2). Mature human NrCAM is an approximately 200 kDa molecule that consists of a 1143 amino acid (aa) extracellular domain (ECD) with 6 Ig-like domains followed by 5 fibronectin type III domains; a 23 aa transmembrane segment, and a 114 aa cytoplasmic domain (3). Within the region of Ig-like domains, human NrCAM shares 92% aa sequence identity with mouse and rat NrCAM. Alternative splicing generates additional isoforms with deletions in the juxtamembrane region of the ECD plus short deletions near the N-terminus, between the 2nd and 3rd Ig-like domains, or following the 6th Ig-like domain. A 140 kDa soluble fragment of the ECD can be released by proteolytic cleavage (4, 5). NrCAM is expressed on cerebellar granule neurons, retinal ganglion cells (RGC), star pyramidal cells in visual cortex, thalamocortical axons, and glial cells (4, 6-11). It is found on both axons and dendritic spines (7, 9). NrCAM mediates homophilic adhesion as well as heterophilic adhesion with Contactin, Contactin-2/TAG1, Neurofascin, PTP beta zeta, and Integrin  alpha 4 beta 1 (5, 12-15) and also interacts with Neuropilin-2, Plexin A3, and EphB2 (8-10). Depending on its interacting partners, NrCAM can promote or inhibit axon and neurite extension (6, 7, 11, 15) and mediate Semaphorin 3F induced neuronal growth cone collapse (9, 10). NrCAM plays an important role in the development of normal vision by regulating RGC axon pathfinding and mapping to the visual cortex (7, 8, 10). It is up-regulated in papillary thyroid carcinomas and the shed form can promote tumorigenesis (5, 16).

  1. Sakurai, T. (2012) Mol. Cell. Neurosci. 49:351.
  2. Stoeckli, E.T. and L.T. Landmesser (1995) Neruon 14:1165.
  3. Lane, R.P. et al. (1996) Genomics 35:456.
  4. Sakurai, T. et al. (2001) J. Cell Bio. 154:1259.
  5. Conacci-Sorrell, M. et al. (2005) Cancer Res. 65:11605.
  6. Faivre-Sarrailh, C. et al. (1999) J. Cell Sci. 112:3015.
  7. Zelina, P. et al. (2005) Development 132:3609.
  8. Dai, J. et al. (2013) PLoS One 8:e73000.
  9. Demyanenko, G.P. et al. (2014) J. Neurosci. 34:11274.
  10. Demyanenko, G.P. et al. (2011) J. Neurosci. 31:1545.
  11. Feinberg, K. et al. (2010) Neuron 65:490.
  12. Mauro, V.P. et al. (1992) J. Cell Biol. 119:191.
  13. Sakurai, T. et al. (1997) J. Cell Biol. 136:907.
  14. Lustig, M. et al. (1999) Dev. Biol. 209:340.
  15. Volkmer, H. et al. (1996) J. Cell Biol. 135:1059.
  16. Gorka, B. et al. (2007) Br. J. Cancer 97:531.
Long Name
Neuronal Cell Adhesion Molecule
Entrez Gene IDs
4897 (Human); 319504 (Mouse)
Alternate Names
Bravo; hBravo; KIAA0343Neuronal surface protein Bravo; MGC138845; MGC138846; neuronal cell adhesion molecule; NgCAM-related cell adhesion molecule; ng-CAM-related; NrCAM; nr-CAM


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