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Your Position: Home > Claudin-9

Claudin-9

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

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Cat. No. Species Product Description Structure Purity Feature
CL9-H5283 Human Human Claudin-9 / CLDN9 Full Length Protein, His,Twin-Strep Tag (Nanodisc)
CL9-H5283-structure
CL9-H5283-sds
CL9-H85D3 Human Biotinylated Human Claudin-9 Full Length Protein, His,Flag Tag&Avitag™ (Detergent)
CL9-H85D3-structure
CHEK-ATP139 Human HEK293/Human Claudin-9 Stable Cell Line
CL9-H52P5 Human Human Claudin-9 / CLDN9 Full Length Protein (VLP)
CL9-H5586 Human Human Claudin-9 / CLDN9 Protein, His,Twin-Strep Tag (Detergent)
CL9-H5586-structure
CL9-H5586-sds
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Part of Bioactivity data

CL9-H52P5-SPR
Claudin-9 SPR

Human Claudin-9 Full Length Protein-VLP (Cat. No. CL9-H52P5) captured on L1 Chip can bind Anti-Claudin 9 antibody [YD4E9] with an affinity constant of 3.61 nM as determined in a SPR assay (Biacore 8K) (Routinely tested).

Protocol
CL9-H5586-SPR
Claudin-9 SPR

Anti-Claudin 9 antibody captured on Protein G-Series S sensor chip can bind Human Claudin-9, His,Twin-Strep Tag (Cat. No. CL9-H5586) with an affinity constant of 38.8 nM as determined in a SPR assay (in presence of DDM and CHS) (Biacore 8K) (QC tested).

Protocol

Synonym Name

CLDN9

Background

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.

Clinical and Translational Updates

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