Recombinant Human NrCAM Fc Chimera Protein, CF Summary
Details of Functionality |
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. |
Source |
Mouse myeloma cell line, NS0-derived human NrCAM protein
Human NrCAM Leu30-Asn600 (Ala526Pro) Accession # Q14CA1 |
IEGRMD |
Human IgG1 (Pro100-Lys330) |
N-terminus |
|
C-terminus |
|
|
Accession # |
|
N-terminal Sequence |
Leu30 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
NRCAM |
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 |
|
Theoretical MW |
90 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 |
120-130 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 °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 MES and NaCl. |
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 Human NrCAM Fc Chimera Protein, CF
Background
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 2
nd and 3
rd Ig-like domains, or following the 6
th 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).
- Sakurai, T. (2012) Mol. Cell. Neurosci. 49:351.
- Stoeckli, E.T. and L.T. Landmesser (1995) Neruon 14:1165.
- Lane, R.P. et al. (1996) Genomics 35:456.
- Sakurai, T. et al. (2001) J. Cell Bio. 154:1259.
- Conacci-Sorrell, M. et al. (2005) Cancer Res. 65:11605.
- Faivre-Sarrailh, C. et al. (1999) J. Cell Sci. 112:3015.
- Zelina, P. et al. (2005) Development 132:3609.
- Dai, J. et al. (2013) PLoS One 8:e73000.
- Demyanenko, G.P. et al. (2014) J. Neurosci. 34:11274.
- Demyanenko, G.P. et al. (2011) J. Neurosci. 31:1545.
- Feinberg, K. et al. (2010) Neuron 65:490.
- Mauro, V.P. et al. (1992) J. Cell Biol. 119:191.
- Sakurai, T. et al. (1997) J. Cell Biol. 136:907.
- Lustig, M. et al. (1999) Dev. Biol. 209:340.
- Volkmer, H. et al. (1996) J. Cell Biol. 135:1059.
- Gorka, B. et al. (2007) Br. J. Cancer 97:531.
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