Sclerostin functions as a potent inhibitor of Wnt signaling and bone formation, making it a critical target for understanding skeletal homeostasis and therapeutic antibody development. This full-length mature protein (aa 24–213) demonstrates robust binding activity with an EC50 of 3.442–3.726 ng/mL in functional ELISA and a binding affinity of 0.324 nM by surface plasmon resonance, providing quantitative benchmarks that support its use in antibody screening, epitope mapping, and competitive binding studies. Mammalian expression preserves the native disulfide bond architecture essential for sclerostin's cystine-knot structure and receptor recognition. With purity exceeding 95% and endotoxin levels below 1.0 EU/μg, this protein meets the quality thresholds commonly required for cell-based Wnt reporter assays and serves as a suitable positive control in immunoassays targeting the SOST pathway.
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