The Y340F point mutation in this TGF-β3 construct enables researchers to dissect structure-function relationships at a specific residue within the mature signaling domain (aa 301–412), providing a precise tool for receptor-ligand binding studies and competition assays using SPR or ELISA. Validated with an ED50 of 10–80 pg/mL in inhibiting IL-4-dependent TF-1 cell proliferation, this protein demonstrates potent bioactivity appropriate for cell proliferation and survival assays, stem cell or osteogenic differentiation studies, and in vivo tumor biology models. Mammalian cell expression preserves native-like glycosylation and folding critical for TGF-β3 receptor engagement, while the tag-free format eliminates potential interference in sensitive functional readouts. Purity exceeding 95% by SDS-PAGE combined with endotoxin levels below 1.0 EU/μg satisfies the quality criteria typical for cell-based assays and downstream in vivo applications in cancer research.
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