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Figure 2 | Proteome Science

Figure 2

From: Increase in local protein concentration by field-inversion gel electrophoresis

Figure 2

Increased local concentrations of protein bands upon pulsing. Protein band intensity analyses in FIGE (a I), CFE (a II), and CFE followed by resting within glass plates in room temperature for 12 hours (a III). Lanes 1 to 6 are 2 μL, 4 μL, 6 μL, 8 μL, 10 μL, and 12 μL of Mark12 protein standards, respectively, in a self-cast Bio-Rad 14% SDS-PAGE 1 mm × 7 cm gel followed by Coomassie blue staining. a I) Gel was run with a pulsed-field at (4 sec/3.4 sec) at 200 V for 13 hours, with an average buffer temperature of 30°C. A II) Gel was run at a constant field of 200 V for one hour and an average buffer temperature of 25°C. a III) Gel was run at a constant field of 200 V for one hour and left at rest for another 12 hours within the glass plates to permit diffusion prior to staining. b) Densitometry analysis of protein bands in the gels of the three conditions tested. Molecular mass was represented by alphabet A to K, where A = 200 kDa, B = 116.3 kDa, C = 97.4 kDa, D = 66.3 kDa, E = 55.4 kDa, F = 36.3 kDa, G = 31.0 kDa, H = 21.5 kDa, I = 14.4 kDa, J = 6.0 kDa, and K = unresolved 3.5/2.0 kDa bands, respectively. Migration distance relative to the dye front (Rf) and intensity of bands from lane 6 of all three gels was densitometrically analyzed using Quantity One software. The graph results were the average of two independent experiments. The graph results were subsequently employed in the calculation of peak variance, σ2, in Table 1.

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