American Society of Hematology

Fig. 3.

$Fig. 3. Interaction of GMR- with GRAP. / COS cells were cotransfected with plasmids encoding the wild type of GMR-α and the fusion protein EGFP-GRAP or EGFP as indicated. Cells were lysed, and proteins were immunoprecipitated with anti-GMR-α sera. Immunoprecipitates were fractionated by 10% SDS-PAGE and immunoblotted. Primary antibodies were polyclonal anti-GMR-α and monoclonal EGFP. The secondary antibody was horseradish peroxidase-linked antirabbit or antimouse immunoglobulin. (A) Cell lysates from cells transfected with GMR-α and EGFP-GRAP or EGFP. Immunoprecipitation with anti-GMR-α and immunoblotting with anti EGFP. (B) No immunoprecipitation. Immunoblotting was with anti-EGFP. (C) Immunoprecipitation and immunoblotting with anti-GMR-α.$

Interaction of GMR- with GRAP.

COS cells were cotransfected with plasmids encoding the wild type of GMR-α and the fusion protein EGFP-GRAP or EGFP as indicated. Cells were lysed, and proteins were immunoprecipitated with anti-GMR-α sera. Immunoprecipitates were fractionated by 10% SDS-PAGE and immunoblotted. Primary antibodies were polyclonal anti-GMR-α and monoclonal EGFP. The secondary antibody was horseradish peroxidase-linked antirabbit or antimouse immunoglobulin. (A) Cell lysates from cells transfected with GMR-α and EGFP-GRAP or EGFP. Immunoprecipitation with anti-GMR-α and immunoblotting with anti EGFP. (B) No immunoprecipitation. Immunoblotting was with anti-EGFP. (C) Immunoprecipitation and immunoblotting with anti-GMR-α.

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