anti-Cdh2 (zebrafish), mAb (rec.) (SH1352-G9)

The cadherin superfamily of cell adhesion molecules regulate cell-cell interaction and are key factors in developmental morphogenesis and tissue repair. Cadherin-2 (N-cadherin; Cdh2), expressed in the vertebrate nervous system, is a type I transmembrane glycoprotein expressed in fusion to an N-terminal propeptide, necessary to avoid intracellular interaction of the molecule. Mature Cdh2 consists of five extracellular immunoglobulin (Ig)-like domains (Cdh2-ECDs), a single-pass transmembrane region and an intracellular domain for the interaction with the cell cytoskeleton, mainly mediated by β-catenin binding. Throughout the early developmental stages of vertebrates, Cdh2 is expressed almost ubiquitously. Later stages its expression seems to be restricted to the central nervous system (CNS) in specific neuronal populations, but it also persists in cardiac muscle. In the central and peripheral nervous systems, Cdh2-dependent cell-cell interactions mediate a variety of neurodevelopmental processes including tissue architecture formation, neuronal migration, axon outgrowth, target recognition and synaptogenesis. Cdh2 levels are often increased during cancer invasion and metastatic behavior resulting in enhanced cell motility. For its role in tumor progression, Cdh2 has been considered a potential biomarker for the prediction of metastases and as an important prognostic factor. As a member of the cadherin superfamily of proteins, zebrafish Cdh2 (zCdh2) shares a high degree of amino acid homology with other members of this family. Zebrafish (Danio rerio) Cdh2-ECD has an overall amino acid identity of 63% to zebrafish Cadherin-4-ECD, with a peak of 68% in domains 1. The Ig-like structure of the 5 extracellular domains and the high sequence similarity to other cadherins requires a careful process of antibody generation against the zCdh2-ECD to avoid unwanted cross-reactivities and a thorough process of binding specificity characterization.