Hello,
I have recently run a western of Vero cells for ACE2. I detected ACE2 at the correct size, but it presents as a double band. The sample was prepared by lysing cells in 1X Laemmli buffer followed by boiling for ten minutes. The gel was a 4-20% tris-glycine and the membrane PVDF. Has anyone observed a similar phenomenon? Could this be a post-translational modification of ACE2 such as glycosylation? Is there anything I should do differently for this protein?
Thank you.
Bill Chi Shun Ho
It could be due to alternative splicing or post-translation modification in certain cell lines. I have seen Western blot of ACE2 from HeLa and Caco-2 cells with double bands too. ACE2 is known to have multiple splice variants.
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