I have read up about stacking and resolving gels but i still dont understand what they are, what they do or their importance in SDS PAGE. Can someone please explain??

thank you
SA

Both Staking and separating are parts of the SDSGEL.
Usualy the Staking made of 4% gel and it is the portion in which the protein samples are loaded.
After the sample finish running this part it enters the separating part in one front. The seprating is the more important part in which the complex of proteins in the sample is separated regarding to their own molecular weight. Usually the staking gel varies in % 4 up to 16% in some case there is a gradient gel that combines % between 4 to 16.
As I mentioned at the beginning the main purpose of SDS Gel is to separate proteins according to their kDa.

Hi again,
I found an interesting article by Ed Rybicki and Maud Purves
Dept Microbiology University of Cape Town
Here is the link
http://www.mcb.uct.ac.za/sdspage.html
Hope it helped
Guy

stacking gel is used to focus the samples in all the wells into a thin band. Think of it as a race, the stacking gel is making sure all the samples are starting at the same point. I am not sure the pure chemistry of it but from a experiment standpoint, that's what the stacking gel is for.

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Hi...
Sorry for the delay..
What you asking is correct? With this you can understand the role of stacking gel.

When the proteins in sample buffer are loaded onto the gel and an electric current is applied, they get trapped in what is termed the moving boundary while migrating through the stacker. Chloride ions from the Tris-HCl in the stacker and the sample buffer form the front part of this boundary, while glycine molecules from the running buffer form the back part of this boundary. The proteins get sandwiched between the chloride ions and the glycine molecules and form a very thin zone, or stack. When this moving boundary reaches the resolving portion of the gel, the difference in pH
between the stacker and the separator causes the glycine molecules to ionize and the glycine ions move through the protein stack right behind the chloride ions. Freed from the moving boundary, the proteins move through the separator, the distance covered being dictated by the size of the protein and the size of the pores in the separator.