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Abstract
Polyclonal antibodies have been raised to synthetic peptides corresponding to several regions of transforming growth factor-β2 (TGF-β2). All antisera were tested for their ability to react with either the native or reduced forms of both TGF-β1 and TGF-β2 in enzyme-linked immunosorbent assays, Western blots, and immunoprecipitation assays. On Western blots, antisera raised to a peptide corresponding to residues 50–75 of TGF-β2 specifically detected 5 ng TGF-β2, while antisera raised to regions 1–30 and 79–108 cross-reacted with TGF-β1. Anti-P 50–75(2) also localized TGF-β2 in murine placenta in immunohistochemical studies. In immunoprecipitation assays with either iodinated TGF-βs or with media conditioned by cells labeled with [35S]Jcysteine, both anti-P 50–75(2) and anti-P 79–108(2) specifically immunoprecipitated TGF-β2 under reducing conditions only, while anti-P 79–108(2) also reacted with TGF-β1. None of the TGF-β2 peptide antibodies was able to block receptor binding of either TGF-β1 or 2. Analysis of the cross-reactivity patterns of these peptide antibodies suggests conformational differences between TGF-β1 and TGF-β2.