Monoclonal Anti-Uvomorulin/E-Cadherin (rat IgG1 isotype) is derived from the DECMA-1 hybridoma, produced by the fusion of rat myeloma cells and splenocytes from an immunized Lou rat. Uvomorulin protein was initially identified in embryonal carcinoma and is identical to E-Cadherin, liver-cell adhesion molecules (L-CAM), Cell CAM 80/120, and Activity-regulated cytoskeleton-associated protein 1 (ARC-1), each of which have been characterized in different systems. Uvomorulin/E-Cadherin has been characterized as a 120 kDa cell surface glycoprotein from which an 84 kDa fragment can be released by trypsin digestion in the presence of Ca2+.
Monoclonal Anti-Uvomorulin/E-Cadherin was selected against the mouse cell adhesion molecule uvomorulin/E-Cadherin. The antibody localizes the cell surface glycoprotein uvomorulin/E-cadherin that has been found to be identical to L-CAM, Cell CAM 80/120, and ARC-1. It blocks both the aggregation of mouse embryonal carcinoma cells and the compaction of pre-implantation embryos. The antibody disrupts confluent monolayers of Madin-Darby canine kidney (MDCK) epithelial cells. In indirect immunofluorescent staining of MDCK cells grown in culture, the antibody shows strong staining on the membrane of adjacent cells, after treatment with 0.5% Triton-X 100.
The antibody localizes the cell surface glycoprotein uvomorulin/E-cadherin that has been found to be identical to L-CAM, Cell CAM 80/120, and ARC-1. The antibody may be used for studies of embryonal development, cell-cell interactions of cultured cells, and localization of uvomorulin/E-cadherin in immunoblotting or immunohistochemical assays.
mouse embryonal carcinoma cell line PCC4 Aza R1.
Monoclonal Anti-Uvomorulin/E-Cadherin has been used in immunofluorescence, immunoblotting, immunoprecipitation, immunohistochemistry, macromolecule permeability assay and agglomeration of two embryoid body assay.
0.2, 0.5 mL
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