Figure 1.
Figure 1. PPARγ protein is expressed in the human megakaryoblast cell line, Meg-01, and by human platelets. (A) Western blot of Meg-01 cell line (15 μg) using a polyclonal anti-PPARγ antibody (Calbiochem). PPARγ bands co-migrated with the human adipose tissue protein extract (15 μg) used as positive control. (B-C) Platelet cell lysates (15 μg) from rigorously purified single donor or pooled platelets were analyzed by Western blot for PPARγ using 2 different anti-PPARγ antibodies (panel B is monoclonal anti-PPARγ [Santa Cruz Biotechnology]; panel C is polyclonal anti-PPARγ [Calbiochem]). Human adipose tissue protein extract (5 μg) was used as positive control (left lane). The PPARγ protein was shown for 3 different single donor and pooled platelet samples. Purified human red blood cells (30 μg) are negative for PPARγ (B). Data are representative of more than 5 experiments.

PPARγ protein is expressed in the human megakaryoblast cell line, Meg-01, and by human platelets. (A) Western blot of Meg-01 cell line (15 μg) using a polyclonal anti-PPARγ antibody (Calbiochem). PPARγ bands co-migrated with the human adipose tissue protein extract (15 μg) used as positive control. (B-C) Platelet cell lysates (15 μg) from rigorously purified single donor or pooled platelets were analyzed by Western blot for PPARγ using 2 different anti-PPARγ antibodies (panel B is monoclonal anti-PPARγ [Santa Cruz Biotechnology]; panel C is polyclonal anti-PPARγ [Calbiochem]). Human adipose tissue protein extract (5 μg) was used as positive control (left lane). The PPARγ protein was shown for 3 different single donor and pooled platelet samples. Purified human red blood cells (30 μg) are negative for PPARγ (B). Data are representative of more than 5 experiments.

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