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. 2003 Sep 1;198(5):831–843. doi: 10.1084/jem.20030574

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Copyright © 2003, The Rockefeller University Press

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Figure 3. — Protein tyrosine phosphorylation of LAT, PLC-γ1, PLC-γ2, and SLP-76 in BMMCs after antigen stimulation. BMMCs were sensitized with 1 μg/ml anti-DNP IgE and stimulated with 100 ng/ml DNP-HSA for 1 min. Lysates (2–4 × 10⁷ cells) were immunoprecipitated with anti-LAT (A), anti–PLC-γ1 (B), anti–PLC-γ2 (C), anti–SLP-76 (D). Immunoprecipitated proteins were resolved by electrophoresis and transferred to nitrocellulose membranes. (A) Tyrosine phosphorylation of LAT and Grb2 association with LAT. After LAT immunoprecipitation, the membrane was immunoblotted with antiphosphotyrosine and anti-Grb2 antibody, and after stripping was reblotted with anti-LAT antiserum. (B) Tyrosine phosphorylation of PLC-γ1 and association of PLC-γ1 and LAT. After PLC-γ1 immunoprecipitation, the membrane was immunoblotted with antiphosphotyrosine, and after stripping, it was reblotted with anti–PLC-γ1. (C) Tyrosine phosphorylation of PLC-γ2 and association PLC-γ2 and LAT. After PLC-γ2 immunoprecipitation, the membrane was immunoblotted with antiphosphotyrosine, and after stripping, it was reblotted with anti–PLC-γ2. (D) Tyrosine phosphorylation of SLP-76. After SLP-76 immunoprecipitation the membrane filter was immunoblotted with antiphosphotyrosine, and after stripping, it was reblotted with anti–SLP-76. Representative data from three or four independent experiments are shown.