| The adoption of cIEF analysis for therapeutic proteins has been gaining popularity within the biopharmaceutical industry. Charge heterogeneity determination adds a critical dimension to establishing identity, purity, post-translational modification and stability of therapeutic protein preparations.
We have undertaken extensive development of cIEF to include optimization of the cartridge aperture, various cIEF chemical components, peptide pI standards, and mobilization technique, paving the way to enhancement of resolution and reproducibility. These system improvements have proven valuable not only in the development of a broad platform method for analysis of monoclonal antibodies (mAbs), but also in the enhancement of narrow range cIEF separation methods. Subsequent intermediate precision studies provide compelling evidence that high performance cIEF separations can be achieved throughout the pH gradient.
|
|
Quick Find
