This purified mouse anti Claudin-5 monoclonal antibody (mAb) is specific to human, mouse, and rat Claudin-5. Anti-Claudin-5 mAb recognizes the expressed product of the CLDN5 gene, also known as Cldn5. The mouse anti Claudin-5 monoclonal antibody is validated for use in applications such as western blot, immunohistochemistry, immunoassay (ELISA), immunocytochemistry/immunofluorescence.
• Applications: Validated applications for mouse anti Claudin-5 monoclonal antibody are western blot, immunohistochemistry, immunoassay (ELISA), immunocytochemistry/immunofluorescence.
• Host Species and Isotype: The host species and isotype of the Claudin-5 monoclonal antibody is mouse IgG1.
• Clone ID of Monoclonal Antibody (mAb): The mouse anti Claudin-5 monoclonal antibody clone is 4C3C2.
• Reactivity: Detects human, rat, and mouse Claudin-5.
• Product Size: Mouse anti Claudin-5 monoclonal 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 are presumed to interact with each other to form a sort of "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 so-called "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. Confinement of the glucose symport to apical surfaces allows glucose to be transported vectorially from the lumen, through the cell, and into the bloodstream.
Initially, the only transmembrane protein known to be associated with tight junctions was occludin, a ~65 kDa protein with four transmembrane domains. Despite widespread expectation to the contrary, a critical structural role for occludin in TJ strands was ruled out by the observation of normal tight junctions formed between cells disrupted at both occludin alleles. Closer examination of isolated tight junctions uncovered two related, ~22 kDa, four-transmembrane domain proteins, 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. 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.