Neurocan, Recombinant, Mouse

Mouse Neurocan is synthesized as a 1268 amino acid (aa) precursor that contains a 22aa signal sequence and a 1246aa mature chain. The mature chain contains one Iglike Vtype domain (aa37 157), two Link domains (aa159 254 and 258 356), two EGFlike domains (aa960 996 and 998 1034), one Ctype lectinlike domain (aa1036 1165), one Sushi domain (aa 1165 1224), and five potential sites for N-linked glycosylation. Mature mouse Neurocan is 90% and 66% aa identical to mature rat and human Neurocan, respectively. Neurocan binds with high affinity to the cell adhesion molecules (CAM) NgCAM and NCAM to inhibit Neuronal adhesion and neurite growth. In the developing rat retina, the expression of Neurocan is regulated both temporally and spatially, which suggests that it may play a role in the differentiation of and neural network formation of the mammalian retina. Injury to the CNS leads to permanent loss of function due to the inability of severed nerve fibers to regenerate back to their targets. The lack of CNS repair is attributed in part to the extracellular matrix chondroitin sulfate proteoglycans, such as Neurocan, which are produced by activated glial cells postinjury.\n\nNeurocan is a chondroitin sulfate proteoglycan of the lectican family and a component of the extracellular matrix of the central nervous system. It is mainly expressed during modeling and remodeling stages of this tissue. Neurocan can bind to various structural extracellular matrix components, such as hyaluronan, heparin, tenascin-C and tenascin-R, and the growth and mobility factors FGF-2, HB-GAM, and amphoterin. Neurocan can also interact with several cell surface molecules, such as N-CAM, L1/Ng-CAM, TAG-1/axonin-1, and an N-cadherin-binding N-acetyl-galactosamine-phosphoryl-transferase, and in vitro studies have shown that neurocan is able to modulate the cell-binding and neurite outgrowth promoting activites of these molecules. Current analysis of the molecular structures and substructures involved in homophilic and heterophilic interactions of these molecules and complementary loss-of-function mutations might shed some light on the roles played by neurocan and interacting molecules in the fine tuning of the nervous system.\n\nRecombinant protein corresponding to aa23-637, expressed in CHO cells with a C-terminal 10 His tag (P55066)\n\nActivity: \nMeasured by the ability of the immobilized protein to enhance the adhesion of H4 human neuroglioma cells, (ATCC: HTB148). When 5x10e4 cells/well are added to mouse Neurocan coated plates, cell adhesion is enhanced in a dose dependent manner. The ED50 for this effect is typically 0.1-0.4ug/ml.\n\nApplications:\nSuitable for use in ELISA. Other applications not tested. \n\nRecommended Dilutions:\nOptimal dilutions to be determined by the resear\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile PBS. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

N2137-04

Size

50ug

Applications

ELISA

Form

Supplied as a lyophilized powder from PBS. Reconstitute with sterile PBS to 0.3mg/ml.

Purity

~95%, by SDS-PAGE under reducing conditions and visualized by silver stain (seen at 120-200kD, reducing conditions). Endotoxin: (same/less than)0.1EU per 1ug (LAL)

References

1. Inatani, M. et al. (1999) Invest. Ophthalmol. Vis. Sci. 40:2350. 2. Friedlander, D.R. et al. (1994) J. Cell Biol. 125:669. 3. Retzler, C. et al. (1996) J. Biol. Chem. 271:27304. 4. Quaglia, X. et al. (2008) Brain 131:240. 5. Ernst, H., et al., J. Cell Science (1995) 108:3807-3816. 6. Balsamo, J., et al., J. Cell Biology (1995) 129:1391-1401.