<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
67 kDa. 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
90-120 kDa, reducing conditions
Publications
Read Publication using 8425-NR in the following applications:
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 with silver staining
Reconstitution Instructions
Reconstitute at 500 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 Mouse NrCAM Protein, CF
Bravo
hBravo
KIAA0343Neuronal surface protein Bravo
MGC138845
MGC138846
neuronal cell adhesion molecule
NgCAM-related cell adhesion molecule
ng-CAM-related
NrCAM
nr-CAM
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 mouse NrCAM is an approximately 200 kDa molecule that consists of a 1090 amino acid (aa) extracellular domain (ECD) with 6 Ig-like domains followed by 4 fibronectin type III domains; a 23 aa transmembrane segment, and a 114 aa cytoplasmic domain. Within the region of Ig-like domains, mouse NrCAM shares 91% and 96% aa sequence identity with human and rat NrCAM, respectively. Alternative splicing generates an additional isoform with short deletions in the sixth Ig-like domain and in the juxtamembrane region of the ECD. A 140 kDa soluble fragment of the ECD can be released by proteolytic cleavage (3, 4). NrCAM is expressed on cerebellar granule neurons, retinal ganglion cells (RGC), star pyramidal cells in visual cortex, thalamocortical axons, and glial cells (3, 5-10). It is found on both axons and dendritic spines (6, 8). NrCAM mediates homophilic adhesion as well as heterophilic adhesion with Contactin, Contactin-2/TAG1, Neurofascin, PTP beta zeta , and Integrin alpha 4 beta 1 (4, 11-14) and also interacts with Neuropilin-2, Plexin A3, and EphB2 (7-9). Depending on its interacting partners, NrCAM can promote or inhibit axon and neurite extension (5, 6, 10, 14) and mediate Semaphorin 3F induced neuronal growth cone collapse (8, 9). NrCAM plays an important role in the development of normal vision by regulating RGC axon pathfinding and mapping to the visual cortex (6, 7, 9). It is upregulated in papillary thyroid carcinomas and the shed form can promote tumorigenesis (4, 15).
Sakurai, T. (2012) Mol. Cell. Neurosci. 49:351.
Stoeckli, E.T. and L.T. Landmesser (1995) Neruon 14:1165.
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.
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