I've been doing a microplate BCA assay (diluting my samples 1:100 or 1:1000) to quantitate proteins before doing Western blots, but I noticed that another lab in my building has a nanodrop. It would save me a few hours each time if I could use the nanodrop to read undiluted 2 uL samples instead of doing the BCA.
I do an acetone precipitation on all my samples and re-suspend them in plain PBS, so I believe that my proteins should be free of any contaminating substances that would absorb at 280 nm. My protein concentration is generally in the 1 - 8 mg/mL range, which I think is okay for the nanodrop?
Can anyone think of a reason why I shouldn't use the nanodrop? I'm only hesitant because no one I know seems to use it, but it might just be because they're afraid of technology.