Antibody refolding
We propose you to refold your denaturated protein.
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Recombinant protein expression in E. Coli has the disadvantage to use detergents (eg : urea) to extract and solubilise proteins. But these conditions have a distorting effect on the proteins obtained.
It is sometimes necessary to remove the denaturant (eg urea) to refold the protein.
Techniques used :
- dialysis
- chromatography buffer exchange
- rapid dilution
- on-column refolding
Note : For all these techniques, the use of various additives in the final buffer is also possible to improve protein solubility and prevent precipitation during the process of removing the denaturing agent. It may be, for example detergents (eg SDS), stabilizers (eg glycerol), chaotropes (eg, urea), salts (eg sodium citrate) or chelators (eg EDTA).
Related services available :
=> Peptide synthesis/Recombinant production
=> Polyclonals production
=> Monoclonals production
=> Antibody labeling
=> Antibody purification
=> Antibody fragmentation
=> Antibody validation