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Description
Cadherins constitute a family of transmembrane glycoproteins involved in Ca2+-dependent cell-cell interactions. The members of this family are differentially expressed in various tissues. They function in the maintenance of tissue integrity and morphogenesis. Cadherins are divided into type I and type II subgroups. Type I cadherins include epithelial cadherin (E-cadherin, cadherin-1 or uvomorulin), neural cadherin (N-cadherin or cadherin-2), placental cadherin (P-cadherin or cadherin-3) and retinal cadherin (R-cadherin or cadherin-4), whereas kidney cadherin (K-cadherin or cadherin-6) and osteoblast cadherin (OB-cadherin or cadherin-11) are type II cadherins. One of the best characterized cadherins is E-cadherin, a 120 kD transmembrane glycoprotein consisting of an 80 kD extracellular and a 40 kD transmembrane and cytoplasmic part. The extracellular domains of E-cadherin are responsible for calcium binding which allows for homophilic interaction with other E-cadherin molecules on the same cell and neighbouring cells. In addition, E-cadherin can interact heterophilically with integrin i!Eic7. The cytoplasmic domain of E-cadherin is linked to the actin cytoskeleton through the associated cytoplasmic catenin proteins, thus establishing a complex localized to adherens junctions. In carcinomas E-cadherin is frequently downregulated, which is consistent with its function of an invasion suppressor in normal epithelia.
Immunogen
5H9 is a mouse monoclonal IgG1 antibody obtained by fusion of P3-X63-Ag 8,653 mouse myeloma cells with spleen cells from a BABL/c mouse immunized with affinity purified 80 kD extracellular fragments of E-cadherin derived from tryptic digestion of A-431 human vulva carcinoma cells.