Hi,

Do you mean some stage of protein expression and purification?

I have no personal experience but It looks like its not so easy to remove tween 80. You can try the pierce columns after diluting your sample (they mention that tween 80 was not tested- www.piercenet.com/files/TR0019-Remove-detergent.pdf).

If its for purification, think it should also work if you dilute the detergent and concentrate proteins with centrifugal filters (egs. Low cut off centricon filters).

Good luck

Manoj

I need to do Hemolytic assay with the culture supernatant. Tween if present will naturally lyse the RBC so i need to remove it

Hi. I am now facing the same problem as you and I need to remove Tween 80 from my culture supernatant.

May I know how did you manage to remove last time?

Hi. The critical micellar concentration (CMC) of tween-80 is ~10 microM so you could use either dialysis or or filters that would retain the large tween-80 micelles while letting proteins go through.

I used to try removing Tween80 from nanoparticle suspension after long time dialysis(MWCO=14000), and I found there left yellow viscous liquid after lyophilization and the mass was quantitatively equal to the initial mass of Tween in the suspension. It means the Tween was not removed at all.

Tween 80 has  a very low CMC of 0.012mM, and a Nagg of 60, so it is very difficult to remove by dialysis or ultra-filtration. See this:

http://wolfson.huji.ac.il/purification/PDF/detergents/PIERCE_DetergentRemoval.pdf