Selectivity: nonspecific non-polar retention mechanism with the surface endcapped to minimize secondary polar silanol interaction
Extraction of hydrophobic molecules from aqueous and biological samples.
Desalting a matrix, as ions are not retained by the sorbent.
Separate large proteins from drugs. The drugs can be extracted from a sample, while macromolecules >15kD are too large to effectively interact with the sorbent.
Selectivity: nonspecific, non-polar retention mechanism with the surface endcapped to minimize secondary polar silanol interactions.
Extracting large hydrophobic molecules (up to 75kD) from water or biological matrices.
Desalting a matrix.
Separate large proteins from drugs. The drugs can be extracted from a sample, while macromolecules >74kD are too large to effectively interact with the sorbent.
Increased extraction efficiency and enhanced clean up of hydrophobic compounds that contain hydroxy or amine functional groups from water or biological fluids.
Desalting a matrix.
Separate large proteins from polar drugs or metabolites. The drugs can be extracted from a sample, while macromolecules >15kD are too large to effectively interact with the sorbent.
Selectivity: combines non-polar retention mechanism via pi-pi and hydrophobic interactions completely free from secondary silanol interactions.
Extraction of non-polar and polar molecules.
Large volume environmental samples.
Extracting large proteins (up to 90kD), which can effectively interact with the large pores of the sorbent, making it useful in applications such as desalting a sample.