Protein stability and storage

By using our UV-fluorescence detector you can measure the stability of your protein in any buffer system using only 40 nL in approximately 5 minutes. You simply load the protein into the Fida 1 instrument, run your experiment and the readout will tell you the size of your protein and, e.g., if there are any aggregates. If the protein structure is known remember to use the PDB correlator to extract information on the oligomeric state of the protein. Read application note for more.

To an extent, yes. FIDA can control the temperature in the Fida Instrument in three different compartments: sample tray, buffer tray and the capillary chamber. In the sample and buffer tray the temperature can be controlled between 5 and 55 degrees Celsius. In the capillary chamber the temperature can be controlled between 10 and 50 degrees Celsius.

You can use the Fida 1 instrument to measure the stability of your protein. This means that you can store your protein in different ways and after storing for some time, check the stability of the protein. The storage method giving the same/similar result as when the protein was freshly prepared will be the most optimal storage condition.

FIDA can measure the unfolding of a protein through chemical denaturation. As we have no limitation on the matrix you measure your sample in we can use various chemical denaturants, such as urea or GnCl, to unfold the proteins.

If a significant size change is caused by the regulations, it can be measured using FIDA. Alternatively, if the regulation is intended to increase affinity toward a target, FIDA can also be used to quantify whether the regulation increased the affinity or not.

There are three independent temperature control: The temperature of the capillary compartment, as well as the two sample trays. The sample trays can be independently set from 5 up to 55 degrees +/- 1 degree. The capillary compartment can be set between 10° Celsius - 55° Celsius. Cooling to 5° Celsius assumes a room temperature at 22° Celsius or below.