CSF-1R orchestrates macrophage differentiation and survival, making its extracellular domain a critical target for interrogating myeloid cell biology and therapeutic intervention in tumor-associated macrophage reprogramming. This construct spans residues 20–511, capturing the complete ligand-binding architecture, and demonstrates quantified binding to recombinant mouse CSF-1 with an EC50 of 3.2–4.3 ng/mL in functional ELISA, providing a validated reagent for competitive inhibition assays, blocking antibody screening, and therapeutic antibody epitope mapping. Mammalian expression ensures native glycosylation and disulfide patterning essential for physiological receptor conformation, supporting high-confidence data in surface plasmon resonance affinity characterization and biolayer interferometry kinetic studies. The protein meets purity and endotoxin criteria typical for ligand-receptor interaction platforms (>90% pure, <1.0 EU/μg), aligning with standards expected in small-molecule inhibitor screening and biologic drug discovery workflows targeting the CSF-1/CSF-1R axis.
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