Epiregulin signals through EGFR and ErbB4 to drive proliferation and autocrine signaling in epithelial and tumor cells, making it a key target in cancer biology research. This tag-free recombinant human proepiregulin fragment (residues 60–108) encompasses the EGF-like domain critical for receptor engagement and demonstrates potent mitogenic activity, with an ED50 below 2 ng/mL in Balb/c 3T3 proliferation assays — corresponding to a specific activity exceeding 5.0 × 10⁵ IU/mg. The E. coli expression system yields a non-glycosylated protein that provides a defined, homogeneous ligand suitable for receptor-ligand binding studies via SPR or ELISA, EGF-family competition assays, and tumor cell proliferation or survival experiments where glycosylation variability could confound results. Purity exceeding 97% by SDS-PAGE combined with endotoxin levels below 1.0 EU/μg supports use in sensitive cell-based assays, including in vitro tumor biology models and antibody characterization workflows.
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