Recombinant CDH17 proteins can support biochemical assessment of antibody binding, specificity, and cross-species reactivity during CDH17-targeted ADC research. Cell-based binding assays are needed to determine whether an antibody recognizes full-length CDH17 in its cell-surface context. ACROBiosystems provides recombinant CDH17 proteins together with a HEK293/Human CDH17 stable cell line with confirmed surface expression for these complementary evaluations.

CDH17 extracellular-region proteins can be used in ELISA, SPR, or BLI assays to assess target binding and, where applicable, binding kinetics or affinity. Domain-specific fragments can further indicate which extracellular region contributes to antibody recognition. His-tagged, Fc-tagged, Avi-tagged, and biotinylated formats allow the protein to be adapted to different capture and detection configurations.

Human CDH17 is used to characterize binding to the human target, while cynomolgus monkey, rhesus macaque, mouse, and rat proteins can be used to examine species cross-reactivity. When comparing binding across species, proteins with comparable domain coverage and tag formats should be selected where possible. This helps reduce assay differences caused by protein format rather than sequence variation.

The appropriate format depends primarily on the immobilization and detection design of the assay. His-tagged proteins provide a relatively small affinity tag, Fc-tagged proteins support Fc-based capture but may affect protein presentation or apparent avidity, and biotinylated proteins enable streptavidin-based immobilization. Potential interference from the tag or capture reagent should also be considered when comparing antibody binding.

A full-length extracellular construct presents the complete extracellular region of CDH17, whereas truncated constructs represent selected regions of the target. Fragments such as CDH17 (129–244), CDH17 (341–449), and CDH17 (450–566) can help determine whether antibody binding is associated with a particular extracellular region. These fragments support domain-level binding analysis but do not independently identify the precise antibody epitope.

CDH17, also known as LI-cadherin, is a cell-surface adhesion protein with an extracellular region containing multiple cadherin domains. Recombinant extracellular CDH17 proteins provide soluble target reagents for studying antibody binding outside the cellular context. ACROBiosystems offers complete extracellular-domain constructs and region-specific fragments for different target characterization needs.