Know #proteinqualityfirst and stop getting inconsistent results
Stop doing unnecessary experiments
Finding out the quality of your protein up front will help you figure out if it’s functional, similar to the previous batch you made, or properly stored. With very little effort, you’ll make sure you’re moving forward with a viable sample, and save yourself from doing have-to-repeat-it-again experiments.
Quickly verify protein quality
Ever wonder if your protein is the same as it was a day or a year ago? Is it even present? Confirm sample quality at any point in your workflow so you know you still have the right protein.
Get answers in minutes
Generate informative data in 3 minutes fast — it makes deciding what to do next that much easier.
Easily analyze any protein sample type
Forget dialyzing or doing sample dilutions. Determine the quality of any protein in any type of buffer over a wide range of concentrations.
Conserve precious sample
Purifying protein for the umpteenth time because you’ve run out of sample is painful. Not only can checking your protein’s quality help you run less experimental parameters later, but it only requires microliters of sample for analysis.
Small benchtop footprint
Save scarce bench space for handwork while getting valuable info from a powerful system with a tiny footprint.
Confirm protein quality with Tycho NT.6
Integrate quality checks into your workflow whenever it makes sense. Not sure why you’re getting inconsistent results even though you followed the same protocol? Check your samples with Tycho. Want to quickly find out if your protein is present? Check your samples with Tycho. You get the picture 🙂 Find out if Tycho is right for you >
How does Tycho identify sample quality?
Tycho verifies protein quality by looking at the structural integrity (or foldedness) of a protein. As a thermal ramp is applied, the changes in the intrinsic fluorescence, detected at both 350 nm and 330 nm, from tryptophan and tyrosine residues in the protein are measured. These changes in fluorescence signal indicate transitions in the folding state of a protein. The temperature at which a transition occurs is called the inflection temperature (Ti). The fluorescence is recorded during the thermal run, plotted as ratio and used to calculate Ti. It’s initial value along with the change in signal over the run (Δ ratio) is also recorded.
Know protein quality early on
During monoclonal antibody therapeutic development, knowing structural integrity as early as possible is one of the strongest indicators of functionality and potential drug efficacy.
A monoclonal antibody (Herceptin) was treated with two oxidation conditions and run on Tycho to test the effects of the treatment on sample quality. A longer oxidation treatment caused more unfolding of the mAb as indicated by the increased initial ratio reading. In addition, increased oxidation treatment causes a left shift in the detected first inflection temperature suggesting possible structural changes to particular domains in the protein (left). MicroScale Thermophoresis (MST) was performed to confirm the effect oxidation treatment can have on Herceptin binding affinity (right).
Find out if Tycho is right for you
Does this ever happen to you?
Learn how knowing protein quality first can prevent unnecessary experiments.