b'NativePAGE Bis-Tris gelsSuperior resolution of native proteins and protein complexesThe Invitrogen NativePAGE Bis-Tris gel system is based on the blue native polyacrylamide gel electrophoresis (BN PAGE) technique that uses Coomassie G-250 dye as a charge shift molecule that binds to proteins and confers a negative charge without denaturing the proteins (Figure 18). This technique overcomes the limitations of traditional native electrophoresis by providing a near-neutral operating pH and detergent compatibility. The near-neutral (pH 7.5) environment of the NativePAGE gel system during electrophoresis results in maximum protein and gel matrix stability, enabling better band resolution than other native gel systems. A gel migration chart is shown in Figure 19.The NativePAGE gel system is designed for: A wide resolving rangefrom 15 kDa to 10 MDa, regardless of isoelectric point Neutral-pH separationthe native state of protein complexes is better preserved Superior performancehigher resolution than Tris-glycine native electrophoresissults acquired witRe hthe Mini Gel TankFigure 18. NativePAGE gel electrophoresis. Two-fold dilution series of protein extracts were run on an Invitrogen NativePAGE 312% Bis-Tris Protein Gel using a Mini Gel Tank. Following electrophoresis, the gel was stained with Coomassie dye and imaged using a flatbed scanner. Lanes 1, 10: blank; lanes 2, 6: 5 L NativeMark Unstained Protein Standard; lanes 35: 10, 5, and 2.5 g spinach chloroplast extract; lanes 79: 10, 5, and 2.5 g bovine mitochondrial extract.Review the protocol for NativePAGE Bis-Tris gels here.Learn more at thermofisher.com/nativepage26'