Fc-linked recombinant proteins for receptor–ligand studies, antibody discovery and assay development.
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Fc fusion proteins join a target domain to an immunoglobulin Fc region. This format can provide dimeric presentation while retaining an Fc region compatible with established capture, detection and interaction workflows.
Target species, Fc species and isotype, expression system and product-specific assay evidence should be reviewed together when selecting a construct.
In acidic endosomes, FcRn binds the Fc region and can route Fc-containing proteins away from lysosomal degradation. Near-neutral pH at the cell surface promotes release after recycling.
This mechanism helps explain why Fc fusion is often selected when longer molecular persistence is useful in therapeutic or diagnostic research contexts.
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Human PD-L1 Protein (PDL1-HP008) was evaluated for binding to anti-PD-L1 antibody–hFc.
Reported EC50: 6.1 ng/mL
Human PD-L1 Protein (PDL1-HP008) was evaluated by SEC-HPLC.
Reported purity: >95%
Rat TIGIT Protein (TIGIT-RP002) was evaluated for binding to Mouse CD155–His.
Reported EC50: 23.1 ng/mL
Mouse CD155–His binding to Rat TIGIT–mFc was evaluated by BLI.
Reported affinity constant: 6.93 nM
Biotinylated Mouse PVRIG Protein (PVRIG-MB001) was evaluated for binding to Mouse Nectin-2–His.
Reported EC50: 5.04 μg/mL
Protein A-captured PVRIG–hFc binding to Mouse Nectin-2–His was evaluated by SPR.
Reported KD: 2.22 μM
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