Claudin-3 is a critical tight junction component frequently overexpressed in ovarian, breast, and colorectal cancers, making it a high-value target for antibody development and tumor metastasis research. This full-length human CLDN3 (residues 1–220) is presented on virus-like particles produced in mammalian cells, preserving the native four-transmembrane topology essential for conformational epitope recognition. Functional ELISA confirms binding to an anti-CLDN3 recombinant antibody with an EC50 of 23.62–34.37 ng/mL, directly supporting antibody screening, validation campaigns, and integrin-ligand or receptor-ligand binding studies where proper extracellular loop presentation is required. The VLP format maintains membrane protein orientation suitable for cell migration and invasion assay development, and endotoxin levels below 1.0 EU/μg align with standards expected in immune cell trafficking experiments and functional screening workflows.
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By Anonymous
Could you kindly tell me the purification method of CSB-MP005505HU (Recombinant Human Claudin-3(CLDN3)-VLPs (Active)).
If a virus was used or not and what kind?
The purification method we usually use is Ultracentrifugation + affinity purification.
VLPs (Virus Like Particles) are nanoscale particles formed by the automatic assembly of one or more capsid proteins of enveloped viruses. VLP particles do not contain viral nucleic acid, cannot replicate autonomously, are highly safe, and have an overall structure similar to virus particles.
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