Monoclonal antibodies recognizing transforming growth factor-<i>beta</i>. Bioactivity neutralization and transforming growth factor <i>beta</i> 2 affinity purification.

James R. Dasch, Doran R. Pace, Wendy Waegell, D Inenaga, LW Ellingsworth

The Journal of Immunology · 1989 · 294 citations · 0 references

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Abstract

Four mAb able to recognize transforming growth factor-beta 2 (TGF-beta)2 were obtained. One of these mAb, 1D11.16, was able to neutralize the biological activity of both TGF-beta 1 and beta 2 in vitro. This was demonstrated in an Il-1, PHA-dependent thymocyte mitogenic assay that is inhibitable by TGF-beta in a dose-dependent manner. All four mAb recognized the dimeric form of TGF-beta 2 in Western blots. The mAb were also found to immunoprecipitate [125I]-TGF-beta 2. mAb 3C7.14 coupled to Sepharose could efficiently immunoaffinity purify TGF-beta 2 from a complex mixture of proteins. Affinity constants were determined for the four mAb and they ranged from 3.4 x 10(8) to 1.6 x 10(7) L/mol.