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. 1998 Aug 3;188(3):505–514. doi: 10.1084/jem.188.3.505

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Presence of tyrosine-phosphorylated cytoskeletal proteins in H. vermiformis. Phosphotyrosine immunoprecipitates (PY/IP) of resting H. vermiformis were resolved under SDS-PAGE conditions and immunoblotted with antibodies to actin, paxillin, vinculin, or pp125^FAK, followed by appropriate HRP-conjugated secondary antibodies (A–D). Total cell lysates from 10⁷ murine splenic B lymphocytes (M) was used as a positive control for comparison, except in A where total cell lysate from H. vermiformis was used (TCL), since antiactin was amebae specific. Arrowheads indicate the relative positions of the cytoskeletal proteins and asterisks represent other cross-reactive protein bands under these immunoblotting conditions. Results are representative of two independent experiments.

Presence of tyrosine-phosphorylated cytoskeletal proteins in H. vermiformis. Phosphotyrosine immunoprecipitates (PY/IP) of resting H. vermiformis were resolved under SDS-PAGE conditions and immunoblotted with antibodies to actin, paxillin, vinculin, or pp125^FAK, followed by appropriate HRP-conjugated secondary antibodies (A–D). Total cell lysates from 10⁷ murine splenic B lymphocytes (M) was used as a positive control for comparison, except in A where total cell lysate from H. vermiformis was used (TCL), since antiactin was amebae specific. Arrowheads indicate the relative positions of the cytoskeletal proteins and asterisks represent other cross-reactive protein bands under these immunoblotting conditions. Results are representative of two independent experiments.