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1 Tg-HYL to the same extent as that for native hyalin.
2 sion libraries with monoclonal antibodies to hyalin.
3 stituent of the hyaline layer is the protein hyalin, a fibrillar glycoprotein of approximately 330 kD
4 olocalization using a monoclonal antibody to hyalin, a protein packaged specifically in cortical gran
5 e we provide a molecular characterization of hyalin and identify a region of the protein that is impo
6 n addition, we have used the perturbing anti-hyalin antibody mAb183 to show that cell attachment to t
7 cretion of the extracellular matrix protein, hyalin, as a marker for new plasma membrane addition in
15 sive activity is partially blocked by dilute hyalin monoclonal antibody Tg-HYL to the same extent as
20 dulus along with a dramatic reduction in the hyalin protein at the apical ECM, thus implicating the a
21 ome of the classic functions ascribed to the hyalin protein in early development and now enable inves
27 er, cells arrested in M phase do not secrete hyalin, suggesting that mitotic exit is required for new
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