Anti-N-Cadherin Antibody

Cadherins are transmembrane proteins responsible for cell adhesion. Cell adhesion is a crucial feature for the sustainability and maintenance of normal tissue function and three dimensional structure. Cadherins share an extracellular domain consisting of multiple repeats of cadherin-specific motif and are calcium dependent homotypic cell-to-cell adhesion molecules. They are localized mostly in specialized sites called adherence junctions¹.

N-cadherin consists of an amino-terminal external domain with five tandem repeats, a single transmembrane segment, and a cytoplasmic carboxy-terminal domain of approximately 150 amino acids. The intracellular domain of N-cadherin interacts with a group of proteins called catenins that are essential for cadherin-mediated cell adhesion. It is suggested that N-cadherin proteins align in a form of “zipper” when involved in cell adhesion. Cadherins on one cell surface form a series of rigid dimers that attach to equivalent dimers on the opposing cells and lateral motion of these complexes allows the cell junction site to “zip up”¹.

N-cadherin plays a role in tumor metastasis. Unlike E-cadherin that causes tumor metastasis when insufficiently, N-cadherin is involved in tumor metastasis when upregulated. N-cadherin stimulates migration, invasion and metastasis of squamous cell breast cancer and its effects are increased by FGF-2 suggesting that N-cadherin and FGFR-1 synergize and promote aggressive tumor behavior. This synergy also promotes neuronal growth¹. Interestingly, low levels of N-cadherin are associated with a higher invasive capacity of astrocytic glioma by increasing tumor (and normal) cell migration speed and creating a less organized pattern of migration³.