Human/Primate NCAM-1/CD56 Alexa Fluor® 594-conjugated Antibody Summary
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.
Detection of NCAM‑1/CD56 in Human PBMCs by Flow Cytometry. Human peripheral blood mononuclear cells (PBMCs) were stained with Mouse Anti-Human CD3 epsilon APC-conjugated Monoclonal Antibody (Catalog # FAB100A) and either (A) Mouse Anti-Human NCAM-1/CD56 Alexa Fluor® 594-conjugated Monoclonal Antibody (Catalog # FAB2408T) or (B) Mouse IgG2B Isotype Control (Catalog # IC0041T). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
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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