Human NCAM-1/CD56 Biotinylated Antibody Summary
Leu20-Pro603, Glu636-Asn741
Accession # NP_001070150
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of NCAM-1/CD56 in Human Peripheral Blood by Flow Cytometry. Human peripheral blood lymphocytes were stained with Mouse Anti-Human CD3 epsilon APC-conjugated Monoclonal Antibody (FAB100A) and either (A) Rabbit Anti-Human NCAM-1/CD56 Biotinylated Monoclonal Antibody (Catalog # FAB24086B) or (B) Irrelevant antibody followed by PE-conjugated streptavidin (F0040). Staining was performed using our Staining Membrane-associated Proteins.
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Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
Background: NCAM-1/CD56
Neural cell adhesion molecule 1 (NCAM-1) is a multifunctional member of the Ig superfamily. It belongs to a family of membrane-bound glycoproteins that are involved in Ca++ independent cell matrix and homophilic or heterophilic cell-cell interactions. NCAM-1 specifically binds to heparan sulfate proteoglycans (1), the extracellular matrix protein agrin (2), and several chondroitin sulfate proteoglycans that include neurocan and phosphocan (3). There are three main forms of human NCAM-1 that arise by alternate splicing. These are designated NCAM-120/NCAM-1 (761 amino acids [aa]), NCAM‑140 (848 aa), and NCAM-180 (1120 aa). NCAM-120 is GPI-linked, while NCAM‑140 and NCAM-180 are type I transmembrane glycoproteins (4 - 6). Additional alternate splicing adds considerable diversity to all three forms, and extracellular proteolytic processing is possible for NCAM-180 (7 ‑ 8). NCAM-1 is synthesized as a 761 aa preproprecursor that contains a 19 aa signal sequence, a 722 aa GPI-linked mature region, and a 20 aa C-terminal prosegment (4). The molecule contains five C-2 type Ig-like domains and two fibronectin type-III domains. Human to mouse, NCAM-1 is 93% aa identical. NCAM-1 appears to be highly sialylated. The polysialyation of NCAM-1 reduces its adhesive property and increases its neurite outgrowth promoting features (9). NCAM-1 in the adult brain shows a decline of sialylation relative to earlier developmental periods. In regions that retain a high degree of neuronal plasticity, however, the adult brain continues to express polysialylation-NCAM-1, suggesting sialylation of NCAM-1 is involved in regenerative processes and synaptic plasticity (10 - 13).
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- Storms, S.D. and U. Rutishauser (1998) J Biol. Chem. 273:27124.
- Margolis, R.K. et al. (1996) Perspect. Dev. Neurobiol. 3:273.
- Dickson, G. et al. (1987) Cell 50:1119.
- Lanier, L.L. et al. (1991) J. Immunol. 146:4421.
- Hemperly, J.J. et al. (1990) J. Mol. Neurosci. 2:71.
- Rutishauser, U.and C. Goridis (1986) Trends Genet. 2:72.
- Vawter, M.P. et al. (2001) Exp. Neurol. 172:29.
- Rutihauser, U. (1990) Adv. Exp. Med. Biol. 265:179.
- Becker, C.G. et al. (1996) J. Neurosci. Res. 45:143.
- Doherty, P. et al. (1995) J. Neurobiol. 26:437.
- Eckardt, M. et al. (2000) J. Neurosci. 20:5234.
- Muller, D. et al. (1996) Neuron 17:413.
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