Hydrophobic interaction chromatography (HIC) is a technique employed for the segregation of macromolecules by exploiting the reversible interaction between the external hydrophobic region of a biological macromolecule and the hydrophobic ligand of a HIC medium, such as phenyl, octyl, or butyl. The interaction is amplified in the presence of a buffer with a high salt concentration, and conversely reduced with a low salt concentration. As a result, based on the salt concentration in the buffer, the protein with less hydrophobicity tends to elute first, whereas the protein with more hydrophobicity elutes last. This method is gaining popularity over other chromatography methods in both analytical and preparatory scale applications, owing to its usage of a less denaturing environment.

The BcMag™ Phenyl Magnetic Beads are distinguished by their homogeneity and superparamagnetic properties. They possess hydrophobic entities on their exterior that expedite their effectiveness as a chromatographic matrix. These beads are meticulously crafted to allow for manual or automatic purification, desalination, and concentration of proteins or peptides within the femtomolar to picomolar range, consequently eliminating the need for repetitive pipetting and centrifugation procedures that can be laborious and time-consuming. Additionally, the BcMag™ Phenyl Magnetic Beads, like C8 beads, share similar polarity; however, they incorporate an electron-rich aromatic ring, which provides exclusive selectivity and retention.

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