Monoclonal antibodies recognizing transforming growth factor-beta. Bioactivity neutralization and transforming growth factor beta 2 affinity purification.

JR Dasch, DR Pace, W Waegell, D Inenaga… - … (Baltimore, Md.: 1950 …, 1989 - journals.aai.org
JR Dasch, DR Pace, W Waegell, D Inenaga, L Ellingsworth
Journal of immunology (Baltimore, Md.: 1950), 1989journals.aai.org
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 …
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.
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