Abstract
The crossreactivity of monoclonal antibodies (hPRa 1, 2, 3 and 6) generated against human progesterone receptor was examined in six mammalian and an avian species using the techniques of sodium-dodecylsulfate polyacrylamide gel electrophoresis and Western blot analysis. Immunoreactive bands were detected on protein blots of receptor-containing preparations from human endometrial carcinoma grown in nude mice, human T47D breast cancer cells, rabbit, cow and mouse uteri, and chick oviduct. No receptor-associated, immunoreactive bands were detected in rat, guinea pig or hamster uteri. The number and molecular weights of the receptor subunits detected varied between species, and only human progesterone receptor displayed electrophoretic microheterogeneity in its high molecular weight subunit. These data demonstrate that the human progesterone receptor antibodies recognize epitopes not common to all species.
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