CD56, aa1-711, Recombinant, Mouse (NCAM-1, Neural Cell Adhesion Molecule)

Neural cell adhesion molecule 1 is a membrane-bound glycoprotein that plays an important role in nervous system development and function (1, 2). Mature mouse NCAM-1 consists of a 692aa extracellular domain (ECD) with five tandem Ig-like domains and two fibronectin type III domains, an 18aa transmembrane segment, and a 386aa cytoplasmic domain (3). Three major splice variants of NCAM-1 are expressed: the 180kD full length NCAM-180 isoform, the 140kD NCAM-140 isoform which lacks most of the cytoplasmic domain, and the 120kD GPI-anchored NCAM-120 isoform that includes the ECD only. Splicing is tissue specific and developmentally regulated (4-6). Within the ECD, mouse NCAM-1 shares 94% and 95% aa sequence identity with human and rat NCAM-1, respectively. It is expressed on neurons and glial cells, skeletal muscle, and immune NK cells (5, 7-9). NCAM-1 is extensively modified with polysialic acid (PSA) during development, but this addition is decreased in adult tissues (5, 6, 8). Polysialylation of NCAM-1 is retained in the adult hippocampus where it is important for synaptic plasticity and memory formation (10). The PSA moiety also participates in the binding of NCAM-1 to heparan sulfate proteoglycans and NCAM-1 mediated migration of olfactory neurons (11, 12). Proteolytic shedding of NCAM-1 liberates a soluble ECD fragment that can inhibit cortical neurite branching and growth (6). The NCAM-140 isoform is preferentially expressed on NK cells that robustly secrete cytokines upon activation (9, 13). Selective up-regulation of the NCAM-140 isoform in a variety of tumors initiates epithelial-mesenchymal transition (EMT) and promotes tumor cell invasion (14, 15). Finally, NCAM-1 is known to interact with a number of transmembrane and extracellular molecules. NK cell NCAM-1 binds to T cell FGF R1, co-stimulating IL-2 production by T cells (16). NCAM-1 also forms a noncovalent membrane complex with GFRa1, 2 and 4, generating a receptor for GDNF, NTN and PSP, respectively (17). And NCAM-1 is reported to form homophilic trans-interactions, and to interact with L1 CAM in cis, and with HSPGs (agrin and collagen XVIII) in trans. In general, these interactions are involved in cell adhesion, migration, and/or process extension (18).\n\nSource: \nRecombinant corresponding to aa1-711 from mouse CD56, fused with 6-His tag at C-terminal, expressed in mouse myeloma cell line, NSO cells.\n\nMolecular Weight: \n~77.4kD\n\nEndotoxin Level:\n(same/less than)1EU/1ug (LAL)\n\nBiological Activity:\nMeasured by the ability of the immobilized protein to support the adhesion of Neuro-2a mouse neuroblastoma cells (ATCC: CCL-131). When 5x104cells/well are added to mouse NCAM-1 coated plates (25ug/ml with 100ul/well), >20% will adhere after 1 hour incubation at 37 degrees C.\nOptimal dilutions should be determined by each laboratory for each application.\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with 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

C2410-63M

Size

50ug

Form

Supplied as a lyophilized powder in PBS. Reconstitute with PBS to 100ug/ml.

Purity

~95% (SDS-PAGE)

References

1. Schmid, R.S. and P.F. Maness (2008) Curr. Opin. Neurobiol. 18:245. 2. Hansen, S.M. et al. (2008) Cell. Mol. Life Sci. 65:3809. 3. Barthels, D. et al. (1987) EMBO J. 6:907. 4. Gennarini, G. et al. (1986) J. Neurosci. 6:1983. 5. Covault, J. et al. (1986) J. Cell Biol. 102:731. 6. Brennaman, L.H. and P.F. Maness (2008) Mol. Cell. Neurosci. 37:781. 7. Noble, M. et al. (1985) Nature 316:725. 8. Chuong, C.M. and G.M. Edelman (1984) J. Neurosci. 4:2354. 9. Lanier, L.L. et al. (1989) J. Exp. Med. 169:2233. 10. Muller, D. et al. (1996) Neuron 17:413. 11. Storms, S.D. and U. Rutishauser (1998) J. Biol. Chem. 273:27124. 12. Tomasiewicz, H. et al. (1993) Neuron 11:1163. 13. Cooper, M.A et al. (2001) Blood 97:3146. 14. Gattenlohner, S. et al. (2009) Am. J. Pathol. 174:1160. 15. Lehembre, F. et al. (2008) EMBO J. 27:2603. 16. Kos, F.J. & Chin, C.S. (2002) Immunol. Cell Biol. 80:364. 17. Paratcha, G. et al. (2003) Cell 113:867. 18. Nielsen, J. et al. (2010) Adv. Exp. Med. Biol. 663:23.