NanoTemper Technologies Announces Monolith X With Breakthrough Spectral Shift Technology, Enabling Binding Affinity Measurements Where Other Methods Fail
NanoTemper Technologies introduced Monolith X, adding breakthrough Spectral Shift technology to their top-selling Monolith product line, valued by scientists for easy setup of immobilization-free binding affinity measurements and minimal sample requirements. Monolith X combines two biophysical modalities — Spectral Shift and MST — equipping scientists to measure all types of binding interactions they encounter.
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“We hear from scientists that they aren’t able to get binding results. They experience this more and more often — whether it’s with challenging interactions, or samples that are inherently unstable and prone to aggregation, or their target has specific buffer requirements,” shares Tanja Bartoschik, Product Manager at NanoTemper. “Spectral Shift is especially great at handling these types of situations, so we’re excited to finally offer it to scientists to be more successful at measuring binding affinities.”
For other scientists, validating results with more than one method is essential to make informed decisions about their projects. For them, Monolith X is the orthogonal method of choice — not only because it complements SPR results with data free from immobilization bias, but it’s easy to get assays up and running quickly.
Monolith X is the workhorse scientists count on to characterize molecular interactions — even the most challenging ones — without the limitations imposed by other methods.
See why scientists choose Monolith X to measure binding affinities: https://resources.nanotempertech.com/monolith/introducing-monolith-x
About NanoTemper Technologies
Our mission at NanoTemper Technologies is to create biophysical tools for scientists in drug discovery and development who need to tackle challenging characterizations. Working with scientists striving to make a difference in the world gets us excited. If you’re facing challenges with affinity screening, molecular interactions, protein stability, protein expression, or protein quality, let’s talk.
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