I have a random question about the EZQ protein assay. I just used it for the first time and really like it, it suits my test purposes well, as I have samples that contain pigments and phenolic compounds (which should not interfere I hope, compared to BCA assay etc). I was wondering if anyone knows more about the exact mechanism of action. I found that the fluorescence reagent "binds electrostatically to basic amino acids, plus supplemented by additional hydrophobic interactions". Also, when you digest/hydrolyze proteins, will this affect total protein over time? I understand that proteins will be broken down into fragments (and digestion depends on native or unfolded form), but if the EZQ assay accounts for all proteins detectable then the total protein would stay about the same? Or would the EZQ assay not account for any protein fragments? If anyone has experience with that, I appreciate sharing your knowledge.

More Nathalie Plundrich's questions See All
Similar questions and discussions