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. Author manuscript; available in PMC: 2015 May 22.
Published in final edited form as: J Thromb Haemost. 2009 Sep 9;7(11):1886–1896. doi: 10.1111/j.1538-7836.2009.03606.x

Fig. 7.

Fig. 7

ESAM associates with the scaffold protein NHERF-1 in human platelets. (A) Amino acid sequence of the ESAM cytoplasmic tail c-terminus in multiple species. The PDZ domain binding motif is underlined. (B) A PDZ domain array was probed using a GST-ESAM cytoplasmic tail fusion protein as described in Methods. There were several positive hits, including PDZ domain 2 of NHERF-1. (C) A complete list of PDZ domains present on the array. Strongly positive hits are in bold. (D) Top panel: Western blot results demonstrating NHERF-1 and CAL expression in human platelets. MDCK cells expressing human NHERF-1 and human brain lysate were used as positive controls. Bottom panel: Co-immunoprecipitation of ESAM and NHERF-1 in human platelets. Human platelet lysates were subjected to immunoprecipitation with anti-ESAM, anti-NHERF-1 or a non-specific IgG control antibody. The membranes were immunoblotted using an anti-NHERF-1 antibody (for ESAM IP) or an anti-ESAM antibody (NHERF-1 IP). Blots are representative of three independent experiments.