N-Cadherin Antibody (8C11) [Allophycocyanin]

N-Cadherin, also referred to as Neural Cadherin (NCAD) or Cadherin-2 (CHD2), is a 130 kDa protein that is a member of the calcium-dependent adhesion molecule family of classical (type I) cadherins (1-4). Under the CDH2 gene, human N-cadherin is synthesized as a 906 amino acid protein with a theoretical molecular weight of 99.8 kDa (5). The N-cadherin protein structure is similar to other classical type I cadherins including epithelial (E-) cadherin and placental (P-) cadherin (1,2). N-cadherin consists of a 25 amino acid (aa) N-terminal signal peptide and 134 aa pro-peptide, a 565 aa extracellular domain (ECD) with five cadherin repeats, a 21 aa transmembrane segment, and a 161 aa cytoplasmic domain (1-3,5). The ECD of N-cadherin monomers is responsible for homotypic binding through either cis or trans adhesion (2,3).

N-cadherin is expressed on multiple cell types but is most highly expressed by mesenchymal cells and neural tissue (2). Functionally, N-cadherin has a number of roles including maintaining structural integrity and adhesion, cell signaling, and formation of neuronal synapses and the vascular wall (2). The cytoplasmic tail interacts with beta-catenin which then binds with alpha-catenin, forming the cadherin-catenin adhesion complex, an important component of adhesions junctions (1-3). Given its role in adhesion, N-cadherin serves as an indicator of epithelial-to-mesenchymal transition (EMT) (1-4). The loss of E-cadherin during EMT corresponds with an increase in N-cadherin expression (1-4). This "cadherin-switch" is associated with increased migratory and invasive behavior observed in tumor progress (1-4). Proteases including activity of a disintegrin and metalloprotease 10 (ADAM10), matrix metalloproteinases (MMPs), caspase 3, presenilin, and calpain can cleave N-cadherin as a mechanism for regulating Wnt/beta-catenin signaling and inducing oncogenic signals (3,4). In addition to its expression in solid tumors, N-cadherin has been indicated in hematological disorders such as leukemia and multiple myeloma (1). N-cadherin antagonists are currently being studied as potential therapeutics for a variety of cancer studies (1-2).

References

1. Mrozik, K. M., Blaschuk, O. W., Cheong, C. M., Zannettino, A., & Vandyke, K. (2018). N-cadherin in cancer metastasis, its emerging role in haematological malignancies and potential as a therapeutic target in cancer. BMC Cancer. https://doi.org/10.1186/s12885-018-4845-0

2. Loh, C. Y., Chai, J. Y., Tang, T. F., Wong, W. F., Sethi, G., Shanmugam, M. K., Chong, P. P., & Looi, C. Y. (2019). The E-Cadherin and N-Cadherin Switch in Epithelial-to-Mesenchymal Transition: Signaling, Therapeutic Implications, and Challenges. Cells. https://doi.org/10.3390/cells8101118

3. Derycke, L. D., & Bracke, M. E. (2004). N-cadherin in the spotlight of cell-cell adhesion, differentiation, embryogenesis, invasion and signalling. The International Journal of Developmental Biology. https://doi.org/10.1387/ijdb.041793ld

4. Yu, W., Yang, L., Li, T., & Zhang, Y. (2019). Cadherin Signaling in Cancer: Its Functions and Role as a Therapeutic Target. Frontiers in Oncology. https://doi.org/10.3389/fonc.2019.00989

5. Unitprot (P1903)

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Array NBP2-54523APC

• N-Cadherin Antibodies
• N-Cadherin ELISA Kits
• N-Cadherin Lysate
• N-Cadherin Proteins
• N-Cadherin ELISA
• N-Cadherin Proteins and Enzymes