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. 2011 Aug;59(8):741–749. doi: 10.1369/0022155411411303

Figure 1.

Figure 1.

Characterization of the anti-phostensin monoclonal antibody, PT2. (A) PT2 binds to full-length trx-phostensin and to residues 1–129 but not to residues 1–39, residues 1–88, or residues 125–165, as observed by Western blot analysis. An aliquot (100 ng) of each protein was loaded onto SDS-PAGE gels (12.5%) and analyzed by Western blot using the anti-phostensin monoclonal antibody, PT2. (B) PT2 antibodies bound to proteins on the membrane from (A) were stripped (in 0.5 M acetic acid plus 0.5 M NaCl) for 30 min, and the membranes were reblotted with anti-trx antibody. All loaded proteins contained a trx fragment. (C) Phostensin is present in human PBMCs. Cellular proteins were extracted by 1% SDS and ultrasonication. An aliquot (100 µg) of crude extract was analyzed by SDS-PAGE (12.5%), transferred onto polyvinylidene difluoride membranes, and blotted with PT2 (1:2000). The molecular weight of phostensin was observed to be 26 kDa.