Measured by the ability of the immobilized protein to enhance the adhesion of H4 human neuroglioma cells. When 5 x 104 cells per well are added to recombinant human Neurocan coated plates, cell adhesion is enhanced in a dose dependent manner. The ED50 for this effect is 50‑200 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human Neurocan protein Glu23-Cys1321, with a C-terminal 6-His tag
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
141.5 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
140-290 kDa, reducing conditions
Publications
Read Publications using 6508-NC 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
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Neurocan Protein, CF
chondroitin sulfate proteoglycan 3 (neurocan)
Chondroitin sulfate proteoglycan 3
CSPG3
CSPG3neurocan core protein
FLJ44681
NCAN
NEUR
neurocan proteoglycan
Neurocan
Background
Neurocan, also known as CSPG3 and 1D1, is a secreted chondroitin sulfate proteoglycan that is primarily expressed in the central nervous system (1). Human Neurocan contains one Ig-like V-type domain, two Link domains, two EGF-like domains, one C-type lectin-like domain, and one Sushi domain (2). It is an approximately 300 kDa molecule of which 66 kDa is chondroitin sulfate and 60 kDa is N‑ and O‑linked glycosylation (3). Mature human Neurocan shares 66% aa sequence identity with mature mouse and rat Neurocan. Human Neurocan is predicted to be cleaved following Met635, resulting in N-terminal (Neurocan-130) and C-terminal (Neurocan-C) fragments whose core glycoproteins are 130 kDa and 150 kDa, respectively (4, 5). The full length molecule is expressed in the developing and juvenile brain, while its cleavage products are found throughout adulthood (3, 4). Neurocan and Neurocan-C are produced by astrocytes and accumulate in the matrix surrounding axonal bundles and neuronal cell bodies; Neurocan-130 is found mainly in the glial cell cytoplasm (6 - 8). Following brain injury, reactive astrocytes deposit increased amounts of Neurocan in the glial scar where it impedes axonal regeneration (6, 9). Neurocan inhibits neuronal adhesion and neurite outgrowth through interactions with a variety of matrix and transmembrane molecules including NCAM-L1, NCAM-1, Syndecan-3, Glypican-1, Tenascin, Contactin-2/TAG1, and HAPLN1 (1, 6, 10 - 15).
Rauch, U. et al. (2001) Cell. Mol. Life Sci. 58:1842.
Prange, C.K. et al. (1998) Gene 221:199.
Rauch, U. et al. (1991) J. Biol. Chem. 266:14785.
Matsui, F. et al. (1994) Neurochem. Int. 25:425.
Rauch, U. et al. (1992) J. Biol. Chem. 267:19536.
Asher, R.A. et al. (2000) J. Neurosci. 20:2427.
Matsui, F. et al. (1998) Brain Res. 790:45.
Abaskharoun, M. et al. (2010) Brain Res. 1327:6.
Shen, L.H. et al. (2008) Glia 56:1747.
Friedlander, D.R. et al. (1994) J. Cell Biol. 125:669.
Sango, K. et al. (2003) Exp. Neurol. 182:1.
Akita, K. et al. (2004) Biochem. J. 383:129.
Grumet, M. et al. (1994) J. Biol. Chem. 269:12142.
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