Human Claudin-9 / CLDN9 Full Length Protein (VLP)

Claudin-9 belongs to the claudin family. Claudins constitute integral membrane proteins responsible for solute and electrolyte permeability of the tight junction that serve as a physical barrier to prevent solutes and water from passing freely through the paracellular space between epithelial or endothelial cell sheets. Tight junctions also play a critical role in maintaining cell polarity and signal transductions. Claudin-9 creates charge specific channels in the paracellular space, plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity, is required to preserve sensory cells in the hearing organ because claudin-9-defective tight junctions fail to shield the basolateral side of hair cells from the K+-rich endolymph. Its ion barrier function is essential in the cochlea, but appears to be dispensable in other organs. Is one of the entry cofactors for hepatitis C virus; it enables HCV entry into target cells just as efficiently as CLDN1.

Immobilized Human Claudin-9 Full Length Protein-VLP (Cat. No. CL9-H52P5) at 5 μg/mL (100 μL/well) can bind Monoclonal Anti-Human Claudin 9 antibody, Rat IgG with a linear range of 0.01-0.156 μg/mL (QC tested).