TGF-β1 serves as a master regulator of immune suppression and tumor microenvironment remodeling, making precise bioactivity essential for meaningful in vitro and in vivo cancer biology studies. This tag-free recombinant human TGF-β1, spanning the mature signaling domain (residues 279–390), demonstrates potent receptor-binding activity with an ED50 of 4–40 pg/mL in inhibiting IL-4-dependent TF-1 cell proliferation—a level of potency that supports use in cell proliferation assays, receptor-ligand binding studies via SPR or ELISA, and tumor biology models examining immune evasion or epithelial-mesenchymal transition. Mammalian cell expression preserves native disulfide bonding and folding critical for proper TGF-β receptor engagement, while endotoxin levels below 1.0 EU/μg combined with greater than 95% purity satisfy the criteria typically required for sensitive cell-based differentiation assays and antibody characterization workflows where background interference must remain minimal.
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