Protein electrophoresis - problem
I have a quite simple problem:unsure:
Recently I've run the gel: it was prepared as 12% denaturing SDS PAGE gel. But it didn't look like 12% (it looked as it was more concentrated). Also during transfer to membrane (Western blot) bigger proteins weren't transfered completely. And eventually I had lateral band spreading during electrophoresis (visible on my page ruler) and also on my membrane after signal detection.
I've repeated this experiment - the same samples but on a new gel and then everything went fine.
So question is - what was wrong with the first gel? It polymerized normally. I'm thinking - maybe I added wrong Tris (usually lateral bands spreading results from incorrect salt concentration)?
Will be much grateful if you could help me to explain this :)
|All times are GMT. The time now is 01:46 PM.|
Powered by vBulletin® Version 3.8.4
Copyright ©2000 - 2015, Jelsoft Enterprises Ltd.
Copyright 2005 - 2012 Molecular Station | All Rights Reserved