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Tm & Tagg

Tm & Tagg

Crack stability with Tm and Tagg

Tm

As your protein unfolds and amino acids rearrange, changes in the fluorescence behavior of tryptophan and tyrosine signal conformational changes of your protein. Intrinsic fluorescence is one of the only direct ways to observe the unfolding of a protein, and can do so based only on amino acids rearranging, unlike methods based on light scattering. Changes in fluorescence intensity or a peak shift tell you exactly when your proteins unfold.

Tagg

When that same protein loses its cool and aggregates together — that temperature is your Tagg. Find out how and when your protein aggregates during a thermal ramp, by using SLS at two different wavelengths to detect both small and large particles. Since proteins can unfold and can aggregate, measuring Tm concurrently with Tagg easily determines when an unfolding event leads to aggregation.

Uncle

Uncle measures Tm and Tagg at the same time and gets answers on protein unfolding and aggregation on up to 48 samples in under 2 hours.  Add a DLS read before the temp ramp to know if you’ve got aggregate trouble right out of the gate. Check out the full-spectrum fluorescence detection if you want to use a dye, or to be sure your formulation isn’t adding fluorescence of its own.