Improving Charge Variant Analysis with Maurice Native Fluorescence
Most post-translational and degradation events affect the biological activity of therapeutic proteins, making charge heterogeneity analysis a critical quality attribute for molecule characterization. Both iCE280 and iCE3 use protein absorption at 280 nm to monitor charge heterogeneity, and now Maurice adds native fluorescence detection to greatly increase cIEF capabilities.
Maurice’s native fluorescence detection for cIEF works by measuring the fluorescence emission of tryptophan’s aromatic group. It’s label-free so you’re not wasting time optimizing protein labeling or dealing with the background noise when label unconjugates from your protein. Baselines are significantly cleaner and less sensitive to ampholyte interference, giving you more options when optimizing your pH gradient.
You'll also get 3-5X more sensitivity compared to UV absorption. That means you can nix concentrating or desalting your samples, decreasing your sample preparation time. And, because proteins tend to aggregate less at lower concentrations, you’ll be able to reduce or even remove urea completely in some of your methods.
Download this app note to learn how Maurice delivers increased sensitivity with a simplified workflow.