Fig. 3.
Fig. 3. Electrophoretic characterization of protein S and binding to C4BP. / (A) The purified wild-type protein S and protein S Heerlen (5 μg/well) were run on 10% SDS-PAGE gels under unreduced and reduced conditions and were visualized with the use of Coomassie Brilliant Blue stain. (B) Binding of wild-type protein S and protein S Heerlen to immobilized C4BP. Purified C4BP was immobilized in microtiter plates. Following the binding of the protein S to the C4BP, the monoclonal antibody (HPS 54) was used to detect the bound protein S. A value of 100% is assigned for the maximum absorbance of wild-type protein S. Means ± SEM of 3 independent experiments performed in duplicate are shown.

Electrophoretic characterization of protein S and binding to C4BP.

(A) The purified wild-type protein S and protein S Heerlen (5 μg/well) were run on 10% SDS-PAGE gels under unreduced and reduced conditions and were visualized with the use of Coomassie Brilliant Blue stain. (B) Binding of wild-type protein S and protein S Heerlen to immobilized C4BP. Purified C4BP was immobilized in microtiter plates. Following the binding of the protein S to the C4BP, the monoclonal antibody (HPS 54) was used to detect the bound protein S. A value of 100% is assigned for the maximum absorbance of wild-type protein S. Means ± SEM of 3 independent experiments performed in duplicate are shown.

Close Modal

or Create an Account

Close Modal
Close Modal