Recombinant Human Claudin-9 (CLDN9)-VLPs (Active)

Claudin-9 plays a critical role in tight junction integrity and has emerged as a target of interest in tumor metastasis research, where its dysregulation influences paracellular permeability and cancer cell invasion. This recombinant human CLDN9 is presented on virus-like particles (VLPs) to preserve native transmembrane topology and conformational epitopes—a key advantage for studying multi-pass membrane proteins that lose structural fidelity when solubilized. Functional ELISA confirms binding to an anti-CLDN6/9 recombinant antibody with an EC50 of 24.93–35.47 ng/mL, supporting use in antibody development and validation, integrin-ligand or selectin-ligand binding studies, and cell migration and invasion assays relevant to metastasis biology. The full-length construct (aa 1–217) with a C-terminal 10xHis tag, expressed in mammalian cells and carrying endotoxin levels below 1.0 EU/μg, provides a suitable basis for functional screening in cancer-focused immunological workflows.