Home > Community > How can I separate LC3A/B I and II bands on western blot?
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Neil Farbstein

How can I separate LC3A/B I and II bands on western blot?

BJ Chippindale  Follow

As Oscar said, Tricine gels work very well in this case. I used it to separate proteins < 15 kDa and to discriminate by 2-3 kDa (in my case, truncated forms of my protein of interest). I used to make a layered gel: stacking at 4%, one upper running portion at 10%, and a lower running portion at 16%. If I remember well, 120 V for 2h should be enough - the running buffer should not get warm. The run is slower than in a 12% gel, but it's worth it.

Please, find the links below:

https://www.ptglab.com/support/western-blot-protocol/tricine-gel-recipe-for-low-molecular-weight-proteins/

http://www.hixonparvo.info/SDS4Peptide.pdf



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Arron Batson  Follow

The electrophoretic mobility of trycine anion is lower than glycine, so sepations of low molecular species are better performed in this buffers system

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Arega Tayu  Follow

Hi Shahid try using a higher concentration of separator gel, 15% or more and run in a Tricine buffer system

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Carolyn Barnett  Follow

The issue is that you are trying to separate low molecular weight protein bands that are close in size. Since 12% acrylamide is not giving you the resolution you need, I suggest you try higher % gels, which means you will have to pour your own, since such gels are unlikely to be commercially available. I've never tried to run protein gels above 12%, but I do know from running DNA sequencing gels, you can go as high as 20%. Since you are running Western blots - as opposed to staining and drying - this should not be a problem. Drying 20% gels is problematic, as they must be soaked in a glycerol solution prior to drying or they will fragment.

There is a lot of literature on analysis of high mobility group [HMG] proteins, which are of similar size to the proteins you are analyzing. I would search that literature to see their methodology for separating small proteins.

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