Jared Head wrote:
>> Here's another question about my Alkaline Phosphatse ELISA.
>> I've just run parallel ELISA plates binding an AP-conjugated antibody to
> its epitope bound to the plate. The only difference between the two
> plates was that in one I bound and then washed the antibody-conjugate with
> PBS, in the other I used PBS/0.1% Tween.
>> I was surprised to see that I got strong binding in the case of the tween,
> but no binding at all with straight PBS. If anything I would have
> expected higher binding *without* the tween due to increased non-specific
> binding. Can anybody explain why tween has increased the binding, and
> ease my confusion?
>> Cheers,
>> Jared
>> --
> Jared Head at the Department of Biochemistry, University of Bristol
>> "A computer lets you make more mistakes faster than any invention in human
> history - with the possible exceptions of handguns and tequila."
> Mitch Ratliffe
tween acts as a surfactant and probably cleans some of the lipid soluble
material prior to the addition of the Ig-congugate, allowing better
binding of the Ig
jim