The 8C11 monoclonal antibody recognizes the extracellular domain of human N-Cadherin (CD325). Cadherins are a family of Ca2+ -dependent intercellular adhesion molecules that play a central role in controlling morphogenetic movements during development. Their function is regulated by association with the actin cytoskeleton by a complex of cytoplasmic proteins called the catenins (α, β, γ). Members of the cadherin family include P-cadherin , E-cadherin (uvomorulin), N-cadherin (neural cadherin), R-cadherin, cadherin 5, L-CAM, and EP-cadherin. N-cadherin mRNA is found at elevated levels in brain and heart and at a much lower level in liver. Mechanisms such as mRNA expression, cytokine modulation, and protease-mediated turnover modulate N-cadherin protein levels during development. In addition, N-cadherin function is indirectly regulated by endogenous kinases and phosphatases. Tyrosine phosphorylation of β-catenin complexed with N-cadherin results in dissociation of N-cadherin from actin. However, N-cadherin also interacts with a PTP1B-like phosphatase that dephosphorylates β-catenin and promotes N-cadherin/actin association. Thus, N-cadherin is an integral adhesion molecule whose function is regulated by protein-protein interactions and phosphorylation/dephosphorylation events.
The antibody was conjugated to BD Horizon BUV615 which is part of the BD Horizon Brilliant™ Ultraviolet family of dyes. This dye is a tandem fluorochrome with an Ex Max near 350 nm and an Em Max near 615 nm. BD Horizon Brilliant BUV615 can be excited by the ultraviolet laser (355 nm) and detected with a 610/20 filter and a 595 nm LP. Due to the excitation of the acceptor dye by the blue/yellow-green laser line, there may be significant spillover into channels detecting PE-CF594 like emissions (eg, 610/20-nm filter).