Claudin-9 is a member of the Claudin family, which consists of integral membrane proteins that regulate solute and electrolyte permeability in tight junctions. These junctions act as physical barriers, preventing solutes and water from freely passing through the paracellular space between epithelial or endothelial cell sheets. Tight junctions are crucial for maintaining cell polarity and facilitating signal transduction.
Claudin-9 is responsible for creating charge-specific channels in the paracellular space and plays a significant role in the tight junction-specific obliteration of the intercellular space through calcium-independent cell-adhesion activity. It is essential for preserving sensory cells in the hearing organ, as claudin-9-defective tight junctions fail to protect the basolateral side of hair cells from the potassium-rich endolymph.
While its ion barrier function is vital in the cochlea, it seems to be unnecessary in other organs. Additionally, Claudin-9 serves as an entry cofactor for the hepatitis C virus, facilitating HCV entry into target cells as efficiently as CLDN1.
Brief information
- Name: Claudin-9
- Target Synonym: DFNB-116, Claudin 9,DFNB116
- Number of Launched Drugs: 0
- Number of Drugs in Clinical Trials: 0
- Lastest Research Phase: Preclinical
Part of bioactivity data
CL9-H52P5-SPR. Image Credit: ACROBiosystems Inc.
The Human Claudin-9 Full Length Protein-VLP (Cat. No. CL9-H52P5) captured on an L1 Chip can bind to the Anti-Claudin 9 antibody [YD4E9] with an affinity constant of 3.61 nM, as determined by an SPR assay (Biacore 8K). This binding interaction is routinely tested.
CL9-H5586-SPR. Image Credit: ACROBiosystems Inc.
The Anti-Claudin 9 antibody, captured on a Protein G-Series S sensor chip, can bind to Human Claudin-9, His, Twin-Strep Tag (Cat. No. CL9-H5586) with an affinity constant of 38.8 nM, as determined by an SPR assay (Biacore 8K) in the presence of DDM and CHS. This binding interaction is routinely tested.
Synonym name