Hej!
I am currently working with Mitofusin-2 protein and I have been using an antibody from Sigma that binds to the N-terminal of the protein and most of the times I see only one band on my WB but once in a while a bunch of bands decide to appear on my membrane. I have read that the protein can be ubiquinated (which explains the upper membranes above the normal MW of the protein) but I cant understand what are the band bellow the 86kDa of the protein.
Does anyone know any paper or have had the same experience as me that could explain this band with a lower molecular weight that the original protein)?
The most likely reason for lower MW bands is proteolysis. Another likely reason is cross-reactivity of the antibody with other proteins in the sample when stringency is compromised. A 3rd possibility is the expression of shorter isoforms of the protein, such as might result from different splicing out of introns from the mRNA. A 4th possibility is a change in post-translational modifications, such as glycosylation (or, less likely, phosphorylation). A 5th possibility is expression of related proteins that cross-react with the antibody.
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