Cadherins comprise a family of Ca2+-dependent adhesion molecules that function to mediate cell-cell binding critical to the maintenance of tissue structure and morphogenesis. The classical cadherins, E-, N- and P-cadherin, consist of large extracellular domains characterized by a series of five homologous NH2 terminal repeats. The most distal of these cadherins is thought to be responsible for binding specificity, transmembrane domains and carboxy terminal intracellular domains. The relatively short intracellular domains interact with a variety of cytoplasmic proteins, such as -catenin, to regulate cadherin function. Members of this family of adhesion proteins include rat cadherin K (and its human homolog, cadherin, R-cadherin, B-cadherin, E/P cadherin and cadherin-5.
Background References
1. Li J et al. Anti-KCNQ1 K+ channel autoantibodies increase IKs current and are associated with QT interval shortening in dilated cardiomyopathy. Cardiovasc Res 98:496-503 (2013).
2. Izumi H & Kaneko Y Evidence of asymmetric cell division and centrosome inheritance in human neuroblastoma cells. Proc Natl Acad Sci U S A 109:18048-53 (2012).
mIHC analysis of mouse liver tissue (Formalin/PFA-fixed paraffin-embedded sections) with Rat anti-Pan-Cadherin antibody (IRS288RT) at 1/100 dilution. The immunostaining was performed with the IRISKitCmTSA Kit (900810). Heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 30 mins at 95℃. DAPI (blue) was used as a nuclear counter stain. Image acquisition was performed with Olympus VS200 Slide Scanner.
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