This purified mouse anti-claudin-5 monoclonal antibody, Alexa Fluor® 488 conjugate, is specific to human, mouse and rat claudin-5. This purified mouse anti-claudin-5 monoclonal antibody, Alexa Fluor® 488 conjugate, recognizes the expressed product of the CLDN5 gene. Conjugated to Alexa Fluor® 488, mouse anti-connexin 30 monoclonal antibody is used in western blotting, ELISA, immunofluorescence, and immunohistochemistry applications.
• Applications: Validated applications for this anti-claudin-5 monoclonal antibody Alexa Fluor® 488 conjugate are western blotting, ELISA, immunofluorescence, and immunohistochemistry.
• Host Species and Isotype: The host species and isotype of the anti-claudin-5 monoclonal antibody is mouse, IgG1.
• Clone ID of Monoclonal Antibody (mAb): The anti-Claudin-5 monoclonal antibody clone is 4C3C2.
• Reactivity: Reacts with human, mouse, and rat.
• Product Size: Rabbit anti-Claudin-5 monoclonal antibody is available in a 100 µg size.
Initially only trans-membrane 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, claudin-1 and claudin-2, with 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 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. The over-expression of Claudin-4 was found to decrease paracellular electrical conductance due to a selective decrease in Na+ permeability, with no significant change for Cl-. Claudin-4 is the first to confer ionic selectivity to paracellular transport, leading to the prediction that the combination of different claudins defines the overall selectivity of different junctions. Thus, Claudin-4 forms channels through the tight junctions that discriminate against Na+ ions and are indifferent to Cl- ions.