Prometheus Panta for protein stability profiling with particle sizing and molecular weight determination by NanoTemper Technologies

Manufacturer NanoTemper Technologies  |  Available Worldwide
Prometheus Panta measures thermal unfolding, particle sizing, and aggregation simultaneously, throughout an entire thermal ramp, for high-resolution stability characterization of proteins. You can determine the molecular weight of your samples, find self-association parameters to predict aggregation propensity, and monitor contaminants in preparations. Prometheus Panta combines DLS, SLS, nanoDSF, and backreflection technologies to give you a detailed profile of your protein’s stability.


Prometheus Panta for protein stability profiling with particle sizing and molecular weight determination by NanoTemper Technologies product image
Prometheus Panta for protein stability profiling with particle sizing and molecular weight determination
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Features:

  • High-resolution information about your protein when you measure thermal unfolding, particle sizing, self-association, and aggregation simultaneously, throughout the entire thermal ramp
  • Flexible throughput, with several options for sample handling
  • Straightforward experimental design, with minimal sample preparation requirements and intuitive software user interface for both running experiments and data analysis

Parameters that Prometheus Panta measures:

Dynamic Light Scattering (DLS)

 

SIZE ANALYSIS

 

Tsize (from growth of rH in cumulants fit): Temperature at which average particle size begins to increase due to unfolding

Average scattering intensity: Identifies if sample concentration is too high or low for proper size distribution analysis

CUMULANT OR SIZE DISTRIBUTION/REGULARIZATION ANALYSIS

rH: Hydrodynamic radius shows size of particle in its solvated state

PDI: Polydispersity index represents distribution of size populations within a sample, and is used to find impurities or poorly folded protein preparations

SELF-INTERACTION ANALYSES

kD: The self-association parameter is used as an indication of a protein’s propensity to aggregate at higher concentrations in a given buffer environment

D0 (*derived from kD analysis): Theoretical diffusion constant at concentration = 0

nanoDSF

 

THERMAL UNFOLDING

 

Tm (for 330 nm, 350 nm, and ratio): Melting temperature, the point at which 50% of a protein is unfolded; higher melting temperatures indicate greater thermal stability

Tonset/Ton (for ratio): Temperature at which unfolding begins; higher Ton values indicate increased thermal stability, and it is considered favorable to have a sharper slope at the unfolding inflection point, which occurs when the Ton is close in value to the Tm

Ea (*derived from thermal unfolding data): Activation energy of unfolding, a parameter that informs on the stability of a protein in a given buffer environment

Reversibility of unfolding: Point at which aggregated protein cannot be recovered and refolded without other chemical means

Backreflection

 

AGGREGATION

 

Tturbidity: Temperature at which large amorphous aggregates (>12.5 nm radius) begin to form in solution

SLS

 

SIZING INFORMATION

 

Molecular weight: Average molecular weight of all particles in solution

SELF-ASSOCIATION AND AGGREGATION PROPENSITY

Tscattering: Temperature at which scattering intensity begins to change, indicating increased size and formation of smaller aggregates

B22: Second virial coefficient ,used to extrapolate self-association behavior at higher concentrations