What does SDS stand for? What is its purpose in this technique?

What is the point of the molecular weight markers?

What is the difference between the stacking gel and the resolving gel? What is its significance?

What is the function of glycerol mixed in with the samples in the stacking gel?

What is the function of the bromophenol blue dye added with the samples?

Towards which electrode do the proteins travel? Why?

Once the plate has been run, the bromophenol blue dye will have separated from the proteins. How are they visualised once again?

What is the general process called when SDS-PAGE is combined with an ELISA in order to produce a 'print' of the electrophoresis gel?

When immunoglobulin samples are run on an electrophoresis plate, why are two protein bands produced?

What is a thick protein band indicative of?

How many heavy, and how many light, chains does a pentameric immunoglobulin (IgM) have?

How many heavy, and how many light, chains does a dimeric immunoglobulin (e.g. IgA) have?

How many heavy, and how many light, chains does a monomeric immunoglobulin (e.g. IgG) have?