|Desmoglein‑2 in MCF‑7 Human Cell Line. Desmoglein‑2 was detected in immersion fixed MCF‑7 human breast cancer cell line using Goat Anti-Human Desmoglein‑2 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF947) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Streptavidin (red; Catalog # NL999) and counterstained with DAPI (blue). Specific staining was localized to the transmembrane region. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.|
Desmoglein-2 is one of three members of the desmoglein subfamily of calcium-dependent cadherin cell adhesion molecules. Together with desmocollins, another subfamily within the cadherin superfamily, the desmoglein isoforms form the adhesive components of desmosomes, the cell-cell adhesive structures that are found in epithelial cells. Human Desmoglein-2 is a type I transmembrane glycoprotein of 1117 amino acid (aa) residues with a 23 aa signal peptide and a 25 aa propeptide. It differs from other classic cadherins by having four instead of five cadherin repeat domains in its extracellular region, and a much larger cytoplasmic region containing five desmoglein repeat domains which share homology with the cadherin repeats. Instead of having the HAV adhesion motif found in type I cadherins, desmogleins have R/YAL as the adhesion motif on its amino-terminal cadherin repeat. The cytoplasmic tails of desmogleins interact with desmoplakins, plakoglobin and plakophilins. In turn, these proteins link the desmogleins with the intermediate filaments. Desmoglein-2 has been shown to be important in establishing cell-cell adhesion and function in epithelial cells. Desmoglein-2 was originally identified in colon carcinoma and colon, and was named HDGC (human desmoglein colon).