This purified rabbit anti-Claudin-3 polyclonal antibody (pAb) is specific to human, mouse and canine Claudin-3 protein. Anti-Claudin-3 pab recognizes the expressed product of the CLDN3 gene, also known as Cldn3. Excitement in the tight junction field continues following the discovery of claudins -3, -4, -5, -6, -7, and -8 and experiments suggesting that tight junctions in different tissues are comprised of different sets of claudin family proteins. Applications in which rabbit anti-Claudin-3 pAb has been used are western blotting, ELISA (native) and immunohistochemistry(FFPE).
• Applications: Validated applications for rabbit anti-Claudin-3 polyclonal antibody are western blotting, ELISA (native), and immunohistochemistry (FFPE).
• Host Species and Isotype: The host species and isotype of the Claudin-3 polyclonal antibody is rabbit IgG.
• Also Known As: Claudin-3 is also known as C7orf1, CPE-R2, CPETR2, HRVP1, RVP1.
• Reactivity: Reacts with human, mouse and canine Claudin-3.
• Product Size: Rabbit anti-Claudin-3 polyclonal antibody is available in a 100 µg pack size.
Tight junctions are specialized regions of cell-cell contact that are particularly abundant in luminal epithelial cell sheets. In freeze-fracture electron micrographs, tight junctions are visualized as belt-like bands of anastomosing sealing strands (TJ strands) that completely encircle the lateral surfaces of each cell. TJ strands on adjacent cells interact with each other to form a "molecular gasket" that prevents ions, water and other molecules from leaking between cells and thus, from one side of the sheet to the other. In addition to this "barrier" function, the "fence" function of tight junctions plays an important role in maintaining epithelial cell-polarity by blocking the diffusion of membrane proteins between apical (luminal) and basolateral cell surfaces. Until recently, the only transmembrane protein known to be associated with tight junctions was occludin, an ~65 kDa protein with four transmembrane domains. Despite widespread expectation, a critical structural role for occludin in TJ strands was ruled out by the observation of apparently normal tight junctions formed between cells disrupted at both occludin alleles. A closer examination of isolated tight junctions uncovered two related ~22 kDa, four-transmembrane domain proteins called claudin-1 and claudin-2, which has no similarity to occludin. In contrast to occludin, which induces only a small number of short strands at cell-cell contact sites when introduced into fibroblasts lacking tight junctions, claudin-1 and -2 induce networks of strands that are characteristic of true tight junctions. Though inconclusive, these findings suggest that claudin-1 and -2 are major structural components of TJ strands and that occludin plays some other accessory role. Excitement in the tight junction field continues to rise following the recent discovery of claudins -3, -4, -5, -6, -7, and -8 and experiments suggesting that tight junctions in different tissues are comprised of different sets of claudin family proteins.