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How does isoelectric focusing separate proteins?
What is a key advantage of using 2D electrophoresis over isoelectric focusing or SDS PAGE alone?
How does 2D electrophoresis separate proteins with identical molecular weights but different isoelectric points?
In a 2D electrophoresis gel, where would you expect to find proteins with high molecular weights and low isoelectric points?
A 2D electrophoresis gel shows a protein spot that is not aligned with others horizontally or vertically. What might this indicate?
In a 2D electrophoresis gel, where would you expect to find proteins with low molecular weights and high isoelectric points?
What is the consequence of incorrect axis labeling in 2D electrophoresis gels?