CCR9 mediates lymphocyte homing to the small intestine and thymus, making it a critical target for understanding mucosal immunity and T-cell trafficking disorders. This full-length receptor (aa 1–369) is presented in virus-like particles that preserve native membrane topology and post-translational modifications, as confirmed by functional ELISA showing specific binding to anti-CCR9 recombinant antibody with an EC50 of 31.67–36.83 ng/mL. The quantified binding activity supports use in competitive inhibition assays for small-molecule antagonist screening, therapeutic antibody epitope mapping, and ligand-receptor interaction studies by surface plasmon resonance or biolayer interferometry. Purity exceeding 95% by SEC-HPLC and endotoxin levels below 1.0 EU/μg align with standards expected in antibody validation workflows and affinity characterization platforms where conformational integrity is non-negotiable.
If in the VLP CCR9 protein the His-tag is expose for the detection
The tag of CSB-MP004848HU is C-terminal 10xHis-tagged. The C-terminal of this protein is in the intracellular region, it is inside the VLPs vesicle structure. So the C-terminal 10xHis-tagged is not exposed.
It can't be detected by his tag under non-denaturing conditions. Under denaturing conditions,after destroying the vesicle structure, it can be detected by his tag.
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