PDGF-BB is a potent mitogen central to tumor microenvironment remodeling, angiogenesis, and stromal cell recruitment, making it a critical tool for in vivo tumor biology models and receptor-ligand interaction studies. This recombinant mouse PDGF-B subunit, covering the full-length mature protein (aa 82–190) with a C-terminal 6xHis tag, demonstrates strong receptor-binding potency with an ED50 of 1.55 ng/mL in Balb/c 3T3 fibroblast proliferation assays, confirming its suitability for cell proliferation and survival experiments as well as PDGFRβ competition binding assays via SPR or ELISA. Expressed in *E. coli*, the protein lacks glycosylation—an advantage for studies requiring homogeneous, non-glycosylated ligand to isolate receptor-binding kinetics from carbohydrate-mediated effects. Purity exceeding 95% by SDS-PAGE combined with endotoxin levels below 1.0 EU/μg satisfies the criteria typical for sensitive cell-based differentiation studies and antibody characterization workflows.
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