Proteomic work can involve the use of two-dimensional polyacrylamide gel electrophoresis (2-D PAGE or 2-DE). In 2-DE, "first dimension" electrophoresis in a polyacrylamide gel with a pH gradient and high urea concentration is followed by a "second dimension" separation in an SDS-PAGE gel.
SDS-PAGE can also be used independently. Proteins and peptides are separated within the gel according to the % acrylamide and crosslinker, given as %T and %C. Typical separations are homogenous: 7% for high mass protein separation and up to 15%T for low mass proteins; 2.7%C; gradient gels can also be run (4-20%T).
Peptides can also be separated using a compatible buffer system. A typical buffer system is Tris/glycine/SDS, however other combinations may be more suitable to your sample. Native and denaturing gels can be prepared. Choice will depend on sample requirements.
