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. 2004 Feb 5;101(7):2040–2045. doi: 10.1073/pnas.0307301101

Fig. 2.

Fig. 2.

Comparison of binding of wild-type and mutant (C257A–C297A) Keap1 to the Neh2 domain of Nrf2. (a) Native gel electrophoresis showing complex between Keap1 (100 pmol) and the Neh2 domain of Nrf2 (10, 20, 40, and 80 pmol, lanes 4–7 and 8–11, respectively). Lane 1, Neh2; lane 2, wild-type Keap1; lane 3, mutant Keap1. Lanes 4–7 show progressively increasing quantities of complex between wild-type Keap1 and Neh2; lanes 8–11 show lower quantities of complex formation between mutant Keap1 and Neh2. Arrowhead, arrow, and asterisk show Keap1, Neh2, and Neh2-Keap1 or mutant Keap1 complex bands, respectively. (b) Densitometric quantification of the intensities of bands of complexes between Neh2 and wild-type Keap1 (black bars) and mutant Keap1 (hatched bars).