For a hi-def look into aggregation, thermodynamics can show whether aggregation is likely and what path proteins will take when aggregating. ΔG is a quantitative stability measurement that describes the ratio of folded to unfolded protein present in a given sample. A protein’s resistance to chemical denaturation can tell you its ΔG. Measure that over multiple concentrations to see what aggregation pathway is thermodynamically favored. If your ΔG stays constant, breathe easy.
Uncle is the one-stop stability platform for biologics. It combines 3 different measurement modes — fluorescence, SLS and DLS — for a whopping total of 12 stability applications on one system. So you can crank out aggregation data with DLS, then stress out your proteins with a heat ramp to look at conformational stability. All the info you’ll get from Uncle makes picking the best formulation, protein, or viral vector a piece of cake.
Stunner is the only system out there that takes Dynamic Light Scattering (DLS) size measurements and UV/Vis concentration from the same sample at the same time. Get a grip on what storage, agitation or a change to your process or formulation does to your protein. See if there’s any aggregation, measure the hydrodynamic size, grab polydispersity when you need to check uniformity, and get the exact concentration while you’re at it.
UV/Vis and DLS also combine to uniquely measure colloidal stability of your samples with kD or B22 data. Instead of making assumptions, Stunner takes an accurate read on concentration for every data point and combines that with DLS data to show how your protein is interacting with itself in solution.
Hunky is the only automated platform for quantifying biologic stability and aggregation pathways with ΔG. Learn, on day one, which protein construct in which formulation has the lowest thermodynamic propensity to aggregate. Quantify your protein’s stability and know if it’s going to aggregate now, not later.