Hello everybody, I am working with the protein streptavidin as linker for coupling experiments. Since streptavidin is very adhesive to reaction tubes (even LowBind) and quite expensive, I was wondering whether Neutravidin is less adhesive, because it is not glycolsated. I am not interested in the binding affinities to specific ligands, but just in non-specific interactions. Does anyone has experience working with Neutravidin and its adhesion behaviour to tubes? Thanks!
Hi Fabian,
I have worked with Neutravidin and never had this kind of problem, at least not with Neutravidin. With other proteins I had sometimes observed a similar phenomen. If it is possible with your down-stream protocol, add a very small amount of detergents, to improve solubility. In my case it was 0,02% Tween 20 (sometimes 0,04%).
Good luck,
Carsten
Hi Carsten,
thank you for sharing your experience. Currently I am using streptavind coupled to gold nanoparticles which leads to the adhesion phenomen especially during centrifugation due to its high mass. Because the streptavidin-gold complexes are very instable, I am not sure, if detergent advantageous. Though, I am going to test adding low concentrated detergent.
Fabian
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