Anti-NECTIN4 / Nectin cell adhesion molecule 4, clone NECTIN4/9906

0.2 mg/ml in 1X PBS with 0.05% BSA, 0.05% sodium azide. Nectin cell adhesion molecule 4 antibody, also known as NECTIN4 antibody, recognizes Nectin cell adhesion molecule 4, a type I transmembrane glycoprotein encoded by the NECTIN4 gene. Commonly referred to as Nectin-4 and also known as Poliovirus receptor related 4 (PVRL4), this protein is a member of the nectin family within the immunoglobulin superfamily. NECTIN4 localizes primarily to the plasma membrane at adherens junctions, where it mediates Ca2+-independent cell-cell adhesion and contributes to epithelial tissue integrity. Nectin cell adhesion molecule 4 antibody is widely used in studies of epithelial organization, cell polarity, and tumor-associated membrane protein expression.NECTIN4 contains three extracellular immunoglobulin-like domains, a single transmembrane region, and a cytoplasmic tail that interacts with intracellular adaptor proteins involved in junction assembly and cytoskeletal linkage. Through homophilic and heterophilic interactions with other nectin family members, Nectin cell adhesion molecule 4 regulates adhesion strength, cell sorting, and tissue morphogenesis. In normal tissues, expression is relatively restricted, with detectable levels in skin, placenta, and select epithelial compartments. During development, nectin family proteins play roles in coordinated cell positioning and junctional maturation.Overexpression of NECTIN4 has been reported in several epithelial malignancies, including urothelial carcinoma, breast cancer, lung cancer, and ovarian cancer. Elevated membrane expression has been associated with enhanced proliferation and tumor progression, supporting its relevance as a biomarker in oncology research. Immunostaining typically demonstrates membranous localization in positive tumor cells, consistent with its function as a cell surface adhesion molecule. Clone NECTIN4/9906 is designed to detect Nectin cell adhesion molecule 4 in research applications and supports investigation of epithelial adhesion dynamics, tumor biology, and membrane-associated signaling pathways.