Recombinant Human IGF-like family receptor 1 (IGFLR1), partial (Active)

IGFLR1 remains a relatively undercharacterized receptor in the IGF-like signaling network, making validated reagents essential for probing its ligand interactions and downstream biology. This recombinant human IGFLR1 encompasses the extracellular domain (aa 23–163) with a C-terminal 6×His tag, expressed in mammalian cells to support native-like glycosylation and proper folding of the ligand-binding region. Functional ELISA confirms that immobilized IGFLR1 at 2 μg/mL binds human IGFL1 with an EC50 of 32.33–47.52 ng/mL, providing a suitable basis for receptor-ligand interaction assays, competitive inhibition studies, blocking antibody screening, and use as a positive control in binding platforms such as SPR and BLI. Purity exceeding 95% by SDS-PAGE combined with endotoxin levels below 1.0 EU/μg satisfies the criteria typical for affinity characterization experiments and early-stage drug discovery screens targeting small-molecule or biologic inhibitors of the IGFLR1–IGFL1 axis.