Protein Reversed-Phase Columns

Reversed-Phase Chromatography

Reversed-phase chromatography of proteins, performed on columns packed with porous or coated, solid-core particles possessing wide pore size particles ( e.g., 300Å), and functionalized with short ligand length chemistries (e.g., C4), is a separation technique based on the ability to separate samples based on relative hydrophobic differences of the proteins in solution. Gradients of increasing organic solvent concentration are frequently used to affect separations in the presence of ion-pairing reagents (e.g., 0.1% TFA or 0.1% formic acid) that minimize undesired ionic interactions. In general, the hydrophobicity of the protein or protein subunit determines the elution order, with the least hydrophobic proteins eluting first. Factors such as particle composition, pore size, ligand type and density, as well as separation conditions (e.g., gradient duration, separation temperature, flow rate) all play important roles in obtaining a separation that meets application requirements.

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