Methods:
1. Gel electrophoresis
2. Size exclusive column
3.Mass spec
Methods:
1.Gel electrophoresis
2.Western blot
3.Column chromatograph(HPLC)
1.Free energy change of protein unfolding, dG and equilibrium constant of a protein between the fold and the unfolded states in solution. This can give an estimation on how much
a protein can resist denaturation conditions such as temperature and urea concentration. It's also a reliable parameter to compare the stability of two proteins. We call it absolute stability.
2.Stability of a protein under practical conditions. This measures changes of a protein structure and function with time under a given condition.It determines half life of an active protein. We call it relative stability.
Some proteins form aggregated oligermer but is still soluble.As a result, this aggregation can not be detected by visual inspection. We offer two methods to determine protein aggregation:
1.Size exclusive chromatograph
2.Dynamic light scatter(DLS)
CD is a commonly used method to determine structure of a protein. It determines
1.Secondary structure, particular alpha helix content in a protein
2.If a protein is unfolded
3.Protein stability
We provide reaserch service to determine protein-ligand interaction.Our main approach is fluorescence, including fluorescence intensity and fluorescence anisotropy (polarization). We determine Kd, Ki (based on competition assay) and IC 50 of binding. Our in-depth knowledge and extensive experience in both data analysis and fluorescence methodology guarantee you a publication quality result.
To request a quote for one of above services, please email us your project to service@ezbiolab.com.
We will return you with a price quote including detailed experimental plan, data analysis method and the
expected results.
