GE and BioRad mini and large format SDS-PAGE systems

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.

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Dr Valerie Wasinger

Dr Valerie Wasinger

Position: Senior Research Scientist
Facility: Bioanalytical Mass Spectrometry Facility
Category: Academic Staff

PT: Tuesday - Friday

Role & Interests

One of the major challenges facing protein analysis is the dynamic range of protein expression within massively complex samples. My interest is in the fractionation and identification of low abundance proteins and peptide and the identification of modified peptides and proteins in complex (1000's proteins) mixtures.

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