Cultivation and characterization of cornea limbal epithelial stem cells on lens capsule in animal material-free medium.
Authors: Albert R, Vereb Z, Csomos K, Moe M, Johnsen E, Olstad O, Nicolaissen B, Rajnavolgyi E, Fesus L, Berta A, Petrovski G
PLoS ONE, 2012;7(10):e47187.
Species: Human
Sample Type: Whole Cells
Application: Flow
Dynamic expression of protective CEACAM1 on melanoma cells during specific immune attack.
Authors: Markel G, Seidman R, Cohen Y, Besser MJ, Sinai TC, Treves AJ, Orenstein A, Berger R, Schachter J
Immunology, 2009;126(2):186-200.
Species: Human
Sample Type: Whole Cells
Application: Flow

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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