SRA 01/04 cells, treated either with 200 μM H2O2 or 1% ERK inhibitor PD98059, as well as controls, and human anterior capsule membrane samples were homogenized and lysed in lysis buffer (20 mM Tris-HCl, 150 mM NaCl, 1% Triton X-100, 1% sodium pyrophosphate, protease inhibitor cocktail). The total protein concentration in the extracts was determined using the BCA reagent (Pierce). Equal amounts of proteins were separated by 15% SDS–PAGE gel, transferred to PVDF membranes, and incubated with appropriate primary and secondary antibodies, following the standard procedures. The primary antibodies were anti-Grx1 (1:1000; 15,804-1-AP, Proteintech), anti-actin (1:60,000; clone AC-74, Sigma), anti-tublin (1:100,000; Calbiochem, Gibbstown, NJ), anti-Bcl (1:500; BD Biosciences, San Diego, CA), anti-Bax (1:5000; Cell Signaling Technology, Danvers, MA), and anti-ERK (1:1000; #4376, Cell Signaling Technology), anti-p-ERK (1:1000; #4370, Cell Signaling Technology), and anti-SOD (1:1000; #2770, Cell Signaling Technology). The secondary antibodies were anti-rabbit or anti-mouse (both from Jackson Laboratories, Bar Harbor, ME). As previously reported [27 (link)], quantitative analysis of the band intensity of the western blots was performed using Image J software (v1.51, National Institutes of Health, Bethesda, MD) to determine changes in the protein levels.