The subunit molecular mass of nitrilase were examined by SDS/PAGE (12% gels) under denaturing conditions, using the proteins of a pre-stained ladder (MBI Fermentas) as reference proteins.
In particular, the model includes a ferro-elasticity effect which is essential for accurate prediction of behavior of pre-stained SMA layers.
Subunit size was determined by 15% SDS-PAGE, using NEB's pre-stained protein ladder.
Size estimation of the developed bands was done using a pre-stained protein ladder (Fermentas, Hanover, MD, USA; catalogue # SM0671).
The molecular masses of proteins from semi-denatured and SDS-PAGE were compared using a pre-stained Roti®-Mark BICOLOR marker (Roth, Karlsruhe, Germany) and a low molecular weight range marker (Sigma, Steinheim, Germany).
Molecular weights were estimated using a pre-stained Roti®-Mark BICOLOR marker.
We used Kaleidoscope Precision Plus Protein and Pre-stained SDS-PAGE Broad Range standards (Bio-Rad) to identify the protein of interest.
Electrophoresis was performed until complete separation of a pre-stained molecular marker (Dual Color, Biorad, Hercules, CA).
The quality of protein transfer was visually checked using pre-stained protein markers (Precision Plus Protein™ All Blue standards, Bio-Rad, Hercules, CA) and staining the membrane with Ponceau S (0.1% [w/v] in 5% [v/v] acetic acid).
One well was loaded with 4 μl of HiMark™ Pre-Stained Protein Standard (Novex®).
