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™ BV786 which is part of the BD Horizon Brilliant™ Violet family of dyes. This dye is a tandem fluorochrome of BD Horizon BV421 with an Ex Max of 405-nm and an acceptor dye with an Em Max at 786-nm. BD Horizon BV786 can be excited by the violet laser and detected in a filter used to detect Cy™7-like dyes (eg, 780/60-nm filter).